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(-) Description

Title :  STRUCTURE OF A PHOSPHOGLUCOSAMINE MUTASE FROM FRANCISELLA TULARENSIS
 
Authors :  J. S. Brunzelle, Z. Wawrzak, T. Skarina, O. Onopriyenko, A. Savchenko, W. F. Anderson
Date :  01 Jul 09  (Deposition) - 19 Jan 10  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.30
Chains :  Asym./Biol. Unit :  A,B
Keywords :  Phosphoglucosamine Mutase, Csgid, Idp02164, Isomerase, Magnesium, Metal-Binding, Phosphoprotein, Structural Genomics, Center For Structural Genomics Of Infectious Diseases (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  J. S. Brunzelle, Z. Wawrzak, T. Skarina, O. Onopriyenko, A. Savchenko W. F. Anderson, Center For Structural Genomics Of Infectious Diseases (Csgid)
Structure Of A Phosphoglucosamine Mutase From Francisella Tularensis
To Be Published
PubMed: search

(-) Compounds

Molecule 1 - PHOSPHOGLUCOSAMINE MUTASE
    ChainsA, B
    EC Number5.4.2.10
    EngineeredYES
    Expression SystemESCHERICHIA COLI BL21(DE3)
    Expression System StrainBL21-CODONPLUS(DE3)-RIPL
    Expression System Taxid469008
    GeneFTT0079, GLMM, MRSA
    Organism ScientificFRANCISELLA TULARENSIS SUBSP. TULARENSIS
    Organism Taxid119856

 Structural Features

(-) Chains, Units

  12
Asymmetric/Biological Unit AB

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (3, 16)

Asymmetric/Biological Unit (3, 16)
No.NameCountTypeFull Name
1MSE12Mod. Amino AcidSELENOMETHIONINE
2SEP2Mod. Amino AcidPHOSPHOSERINE
3ZN2Ligand/IonZINC ION

(-) Sites  (2, 2)

Asymmetric Unit (2, 2)
No.NameEvidenceResiduesDescription
1AC1SOFTWARESEP A:101 , ASP A:239 , ASP A:241 , ASP A:243BINDING SITE FOR RESIDUE ZN A 900
2AC2SOFTWARESEP B:101 , ASP B:239 , ASP B:241 , ASP B:243BINDING SITE FOR RESIDUE ZN B 900

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 3I3W)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 3I3W)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 3I3W)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 3I3W)

(-) Exons   (0, 0)

(no "Exon" information available for 3I3W)

(-) Sequences/Alignments

Asymmetric/Biological Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:441
 aligned with GLMM_FRATT | Q5NII8 from UniProtKB/Swiss-Prot  Length:443

    Alignment length:441
                                    12        22        32        42        52        62        72        82        92       102       112       122       132       142       152       162       172       182       192       202       212       222       232       242       252       262       272       282       292       302       312       322       332       342       352       362       372       382       392       402       412       422       432       442 
           GLMM_FRATT     3 KYFGTDGIRGEVANSTITVEFTQKLGNAVGSLINQKNYPKFVIVGQDTRSSGGFLKFALVSGLNAAGIDVLDLGVVPTPVVAFMTVKHRAAAGFVITASHNKFTDNGIKLFSSNGFKLDDALEEEVEDMIDGDFIYQPQFKFGSYKILANAIDEYIESIYSRFAKFVNYKGKVVVDCAHGAASHNFEALLDKFGINYVSIASNPDGLNINVGCGATCVSNIKKAVKEQKADLGISLDGDADRIIIVDENGQEIDGDGILNILAQYSDICGGTNGIVGTQMTNMSYENHYRANKIPFIRSKVGDRYVLEDLVKYGYKIGGESSGHVINLNFGTTGDGLFTAIQLLAIFSQADKPVSEFKLQGELMQQTLINVPLTKKVAREDLQKVASDVNDVEKRLGNRGRVLLRPSGTEPVLRVMVEADDKSLATNEAEYLVEKVKQKLV 443
               SCOP domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ........eee......hhhhhhhhhhhhhhhhhhh....eeeeee....hhhhhhhhhhhhhhhhh.eeeeeee.hhhhhhhhhhhh...eeeee........eeeeeeee......hhhhhhhhhhhhh.............eee....hhhhhhhhhhhhh.......eeeee.......hhhhhhhhhh..eeee.................hhhhhhhhhhhhh..eeeee......eeee.....eehhhhhhhhhhhh.........eeee...hhhhhhhhhhh...eeee....hhhhhhhhhhh..eee.....eee.......hhhhhhhhhhhhh.....hhhhh.......eeeeeeee.....hhhhhhhhhhhhhhhhhhhh..eeeeeeee..eeeeeeeeee.hhhhhhhhhhhhhhhhhhhh. Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3i3w A   3 KYFGTDGIRGEVANSTITVEFTQKLGNAVGSLINQKNYPKFVIVGQDTRSSGGFLKFALVSGLNAAGIDVLDLGVVPTPVVAFmTVKHRAAAGFVITAsHNKFTDNGIKLFSSNGFKLDDALEEEVEDmIDGDFIYQPQFKFGSYKILANAIDEYIESIYSRFAKFVNYKGKVVVDCAHGAASHNFEALLDKFGINYVSIASNPDGLNINVGCGATCVSNIKKAVKEQKADLGISLDGDADRIIIVDENGQEIDGDGILNILAQYSDICGGTNGIVGTQmTNmSYENHYRANKIPFIRSKVGDRYVLEDLVKYGYKIGGESSGHVINLNFGTTGDGLFTAIQLLAIFSQADKPVSEFKLQGELmQQTLINVPLTKKVAREDLQKVASDVNDVEKRLGNRGRVLLRPSGTEPVLRVmVEADDKSLATNEAEYLVEKVKQKLV 443
                                    12        22        32        42        52        62        72        82   |    92       102       112       122       132       142       152       162       172       182       192       202       212       222       232       242       252       262       272       282  |    292       302       312       322       332       342       352       362   |   372       382       392       402       412     | 422       432       442 
                                                                                                              86-MSE        101-SEP                       131-MSE                                                                                                                                                282-MSE                                                                             366-MSE                                             418-MSE                     
                                                                                                                                                                                                                                                                                                                    285-MSE                                                                                                                                                          

Chain B from PDB  Type:PROTEIN  Length:440
 aligned with GLMM_FRATT | Q5NII8 from UniProtKB/Swiss-Prot  Length:443

    Alignment length:440
                                    12        22        32        42        52        62        72        82        92       102       112       122       132       142       152       162       172       182       192       202       212       222       232       242       252       262       272       282       292       302       312       322       332       342       352       362       372       382       392       402       412       422       432       442
           GLMM_FRATT     3 KYFGTDGIRGEVANSTITVEFTQKLGNAVGSLINQKNYPKFVIVGQDTRSSGGFLKFALVSGLNAAGIDVLDLGVVPTPVVAFMTVKHRAAAGFVITASHNKFTDNGIKLFSSNGFKLDDALEEEVEDMIDGDFIYQPQFKFGSYKILANAIDEYIESIYSRFAKFVNYKGKVVVDCAHGAASHNFEALLDKFGINYVSIASNPDGLNINVGCGATCVSNIKKAVKEQKADLGISLDGDADRIIIVDENGQEIDGDGILNILAQYSDICGGTNGIVGTQMTNMSYENHYRANKIPFIRSKVGDRYVLEDLVKYGYKIGGESSGHVINLNFGTTGDGLFTAIQLLAIFSQADKPVSEFKLQGELMQQTLINVPLTKKVAREDLQKVASDVNDVEKRLGNRGRVLLRPSGTEPVLRVMVEADDKSLATNEAEYLVEKVKQKL 442
               SCOP domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ........eee......hhhhhhhhhhhhhhhhhhhh...eeeeee....hhhhhhhhhhhhhhhhh.eeeeeee.hhhhhhhhhhhh...eeeee........eeeeeeee......hhhhhhhhhhhhh.............eee....hhhhhhhhhhhhh........eeee.......hhhhhhhhhh...eee.................hhhhhhhhhhhh...eeeee......eeee.....eehhhhhhhhhhhh.........eeee...hhhhhhhhhhh...eeee....hhhhhhhhhhh..eee.....eee.......hhhhhhhhhhhhh.....hhhhh.......eeeeeeee............hhhhhhhhhhhhh..eeeeeee.....eeeeeeee.hhhhhhhhhhhhhhhhhhhh Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 3i3w B   3 KYFGTDGIRGEVANSTITVEFTQKLGNAVGSLINQKNYPKFVIVGQDTRSSGGFLKFALVSGLNAAGIDVLDLGVVPTPVVAFmTVKHRAAAGFVITAsHNKFTDNGIKLFSSNGFKLDDALEEEVEDmIDGDFIYQPQFKFGSYKILANAIDEYIESIYSRFAKFVNYKGKVVVDCAHGAASHNFEALLDKFGINYVSIASNPDGLNINVGCGATCVSNIKKAVKEQKADLGISLDGDADRIIIVDENGQEIDGDGILNILAQYSDICGGTNGIVGTQmTNmSYENHYRANKIPFIRSKVGDRYVLEDLVKYGYKIGGESSGHVINLNFGTTGDGLFTAIQLLAIFSQADKPVSEFKLQGELmQQTLINVPLTKKVAREDLQKVASDVNDVEKRLGNRGRVLLRPSGTEPVLRVmVEADDKSLATNEAEYLVEKVKQKL 442
                                    12        22        32        42        52        62        72        82   |    92       102       112       122       132       142       152       162       172       182       192       202       212       222       232       242       252       262       272       282  |    292       302       312       322       332       342       352       362   |   372       382       392       402       412     | 422       432       442
                                                                                                              86-MSE        101-SEP                       131-MSE                                                                                                                                                282-MSE                                                                             366-MSE                                             418-MSE                    
                                                                                                                                                                                                                                                                                                                    285-MSE                                                                                                                                                         

   Legend:   → Mismatch (orange background)
  - → Gap (green background, '-', border residues have a numbering label)
    → Modified Residue (blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 3I3W)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 3I3W)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 3I3W)

(-) Gene Ontology  (7, 7)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A,B   (GLMM_FRATT | Q5NII8)
molecular function
    GO:0016868    intramolecular transferase activity, phosphotransferases    Catalysis of the transfer of a phosphate group from one position to another within a single molecule.
    GO:0016853    isomerase activity    Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
    GO:0000287    magnesium ion binding    Interacting selectively and non-covalently with magnesium (Mg) ions.
    GO:0046872    metal ion binding    Interacting selectively and non-covalently with any metal ion.
    GO:0008966    phosphoglucosamine mutase activity    Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.
biological process
    GO:0005975    carbohydrate metabolic process    The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. Includes the formation of carbohydrate derivatives by the addition of a carbohydrate residue to another molecule.
    GO:0071704    organic substance metabolic process    The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon.

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