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(-) Description

Title :  L-FUCULOSE 1-PHOSPHATE ALDOLASE
 
Authors :  M. A. Higgins, M. D. L. Suits, C. Marsters, A. B. Boraston
Date :  16 Aug 13  (Deposition) - 18 Dec 13  (Release) - 19 Mar 14  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.03
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (4x)
Keywords :  Lyase, Fucose Processing (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  M. A. Higgins, M. D. Suits, C. Marsters, A. B. Boraston
Structural And Functional Analysis Of Fucose-Processing Enzymes From Streptococcus Pneumoniae.
J. Mol. Biol. V. 426 1469 2014
PubMed-ID: 24333485  |  Reference-DOI: 10.1016/J.JMB.2013.12.006

(-) Compounds

Molecule 1 - L-FUCULOSE PHOSPHATE ALDOLASE
    ChainsA
    EC Number4.1.2.17
    EngineeredYES
    Expression SystemESCHERICHIA COLI
    Expression System PlasmidPET28
    Expression System StrainBL21(DE3)
    Expression System Taxid469008
    Expression System Vector TypePLASMID
    Organism CommonPNEUMONOCOCCUS
    Organism ScientificSTREPTOCOCCUS PNEUMONIAE
    Organism Taxid170187
    StrainTIGR4
    SynonymL-FUCULOSE 1-PHOSPHATE ALDOLASE

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit A
Biological Unit 1 (4x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (6, 8)

Asymmetric Unit (6, 8)
No.NameCountTypeFull Name
113P1Ligand/Ion1,3-DIHYDROXYACETONEPHOSPHATE
2EDO3Ligand/Ion1,2-ETHANEDIOL
3GOL1Ligand/IonGLYCEROL
4NI1Ligand/IonNICKEL (II) ION
5SO41Ligand/IonSULFATE ION
6ZN1Ligand/IonZINC ION
Biological Unit 1 (4, 24)
No.NameCountTypeFull Name
113P4Ligand/Ion1,3-DIHYDROXYACETONEPHOSPHATE
2EDO12Ligand/Ion1,2-ETHANEDIOL
3GOL4Ligand/IonGLYCEROL
4NI-1Ligand/IonNICKEL (II) ION
5SO44Ligand/IonSULFATE ION
6ZN-1Ligand/IonZINC ION

(-) Sites  (8, 8)

Asymmetric Unit (8, 8)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLY A:25 , HIS A:93 , HIS A:95 , TYR A:114 , HIS A:155 , 13P A:303BINDING SITE FOR RESIDUE ZN A 301
2AC2SOFTWAREGLY A:-4 , SER A:-3 , HIS A:-2BINDING SITE FOR RESIDUE NI A 302
3AC3SOFTWAREGLY A:25 , GLY A:26 , ASN A:27 , SER A:43 , GLY A:44 , SER A:72 , SER A:73 , GLU A:74 , HIS A:93 , HIS A:95 , TYR A:114 , HIS A:155 , ZN A:301 , HOH A:2021 , HOH A:2101BINDING SITE FOR RESIDUE 13P A 303
4AC4SOFTWAREGLY A:25 , GLY A:26 , ASN A:27 , SER A:43 , GLY A:44 , SER A:72 , SER A:73 , HOH A:2021BINDING SITE FOR RESIDUE SO4 A 304
5AC5SOFTWAREARG A:147BINDING SITE FOR RESIDUE EDO A 305
6AC6SOFTWARETHR A:84 , ARG A:85 , ASP A:86BINDING SITE FOR RESIDUE EDO A 306
7AC7SOFTWAREASN A:63 , VAL A:64 , THR A:84 , HOH A:2078BINDING SITE FOR RESIDUE EDO A 307
8AC8SOFTWARETHR A:133 , LYS A:134 , GLU A:135 , HOH A:2075BINDING SITE FOR RESIDUE GOL A 308

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 4C25)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 4C25)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 4C25)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 4C25)

(-) Exons   (0, 0)

(no "Exon" information available for 4C25)

(-) Sequences/Alignments

Asymmetric 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:212
 aligned with A0A0H2US48_S | A0A0H2US48 from UniProtKB/TrEMBL  Length:212

    Alignment length:212
                                 1                                                                                                                                                                                                              
                                 |   5        15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205  
         A0A0H2US48_S     - -----MSDVKQELIKYGKKLVETDLTKGTGGNLSVFDREKQLMAITPSGIDFFEIKESDIVVMDINGNVVEGERLPSSEWYMHLIQYQTRDDIDAIIHAHTTYATVLACLREPLPASHYMIAVAGKDVRVAEYATYGTKELAVNAAKAMEGRRAVLLANHGILAGAQNLLNAFNIVEEVEYCAKIYCLAKNFGEPVVLPDEEMELMAEKFKT 207
               SCOP domains d4c25a_ A: automated matches                                                                                                                                                                                         SCOP domains
               CATH domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .....hhhhhhhhhhhhhhhhhh........eeeeee....eeee.....hhhhhhhhhheeee....eee.......hhhhhhhhhhhh....eeeee..hhhhhhhhhh......hhhhhhh....eee......hhhhhhhhhhhh....eeee...eeeeee.hhhhhhhhhhhhhhhhhhhhhhhhhh.....hhhhhhhhhhhhhh Sec.struct. author
                 SAPs(SNPs) -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript -------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 4c25 A  -4 GSHMASSDVKQELIKYGKKLVETDLTKGTGGNLSVFDREKQLMAITPSGIDFFEIKESDIVVMDINGNVVEGERLPSSEWYMHLIQYQTRDDIDAIIHAHTTYATVLACLREPLPASHYMIAVAGKDVRVAEYATYGTKELAVNAAKAMEGRRAVLLANHGILAGAQNLLNAFNIVEEVEYCAKIYCLAKNFGEPVVLPDEEMELMAEKFKF 207
                                     5        15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175       185       195       205  

   Legend:   → Mismatch (orange background)
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  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  (1, 1)

Asymmetric Unit

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 4C25)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 4C25)

(-) Gene Ontology  (0, 0)

Asymmetric Unit(hide GO term definitions)
    (no "Gene Ontology" information available for 4C25)

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/TrEMBL
        A0A0H2US48_S | A0A0H2US484c24

(-) Related Entries Specified in the PDB File

4c20 L-FUCOSE ISOMERASE
4c21 L-FUCOSE ISOMERASE IN COMPLEX WITH FUCITOL
4c22 L-FUCOSE ISOMERASE IN COMPLEX WITH FUCULOSE
4c23 L-FUCULOSE KINASE
4c24 L-FUCULOSE 1-PHOSPHATE ALDOLASE