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(-) Description

Title :  ELECTROSTATICS OF ACTIVE SITE MICROENVIRONMENTS FOR E. COLI DHFR
 
Authors :  C. T. Liu, J. P. Layfield, R. J. Stewart Iii, J. B. French, P. Hanoian, J. S. Hammes-Schiffer, S. J. Benkovic
Date :  22 Mar 14  (Deposition) - 16 Jul 14  (Release) - 01 Oct 14  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.26
Chains :  Asym./Biol. Unit :  A
Keywords :  Electrostatics, Catalysis, Oxidoreductase, Dhfr (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  C. T. Liu, J. P. Layfield, R. J. Stewart, J. B. French, P. Hanoian, J. B. Asbury, S. Hammes-Schiffer, S. J. Benkovic
Probing The Electrostatics Of Active Site Microenvironments Along The Catalytic Cycle For Escherichia Coli Dihydrofolat Reductase.
J. Am. Chem. Soc. V. 136 10349 2014
PubMed-ID: 24977791  |  Reference-DOI: 10.1021/JA5038947

(-) Compounds

Molecule 1 - DIHYDROFOLATE REDUCTASE
    Chains: A
    EC Number: 1.5.1.3
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Taxid: 562
    Gene: FOLA, ECS0051, LF82_0721
    Mutation: YES
    Organism Scientific: ESCHERICHIA COLI
    Organism Taxid: 562

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (5, 7)

Asymmetric/Biological Unit (5, 7)
No.NameCountTypeFull Name
1ACT2Ligand/IonACETATE ION
2CA2Ligand/IonCALCIUM ION
3MTX1Ligand/IonMETHOTREXATE
4NAP1Ligand/IonNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
5XCN1Mod. Amino AcidS-CYANO-L-CYSTEINE

(-) Sites  (5, 5)

Asymmetric Unit (5, 5)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREILE A:5 , ALA A:6 , ALA A:7 , MET A:20 , ASP A:27 , PHE A:31 , ILE A:50 , XCN A:54 , ARG A:57 , ILE A:94 , TYR A:100 , NAP A:202 , HOH A:328binding site for residue MTX A 201
2AC2SOFTWAREALA A:6 , ALA A:7 , ILE A:14 , ASN A:18 , ALA A:19 , MET A:20 , GLY A:43 , ARG A:44 , HIS A:45 , THR A:46 , LEU A:62 , SER A:63 , SER A:64 , GLN A:65 , LYS A:76 , ILE A:94 , GLY A:96 , GLY A:97 , ARG A:98 , VAL A:99 , TYR A:100 , GLN A:102 , ASP A:131 , GLU A:139 , MTX A:201 , HOH A:303 , HOH A:315 , HOH A:333binding site for residue NAP A 202
3AC3SOFTWAREASP A:70 , ASP A:87binding site for residue ACT A 203
4AC4SOFTWAREASP A:70binding site for residue ACT A 204
5AC5SOFTWAREASP A:116 , HIS A:149 , ARG A:159 , HOH A:306 , HOH A:324binding site for residue CA A 205

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 4P68)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Gly A:95 -Gly A:96

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 4P68)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 4P68)

(-) Exons   (0, 0)

(no "Exon" information available for 4P68)

(-) 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:159
                                                                                                                                                                                               
               SCOP domains --------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains --------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains --------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .eeeeeeehhh.eee........hhhhhhhhhhhhh...eeeehhhhhhhh.......eeee..........eee.hhhhhhhhh.....eeeeehhhhhhhhhhhh.eeeeeee.......ee........eeeeeeeee.........eeeeeeee. Sec.struct. author
                 SAPs(SNPs) --------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE --------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript --------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 4p68 A   1 MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPxPGRKNIILSSQPGTDDRVTWVKSVDEAIAAAGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYSFEILERR 159
                                    10        20        30        40        50   |    60        70        80        90       100       110       120       130       140       150         
                                                                                54-XCN
   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  (0, 0)

(no "SCOP Domain" information available for 4P68)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 4P68)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 4P68)

(-) Gene Ontology  (9, 9)

Asymmetric/Biological Unit(hide GO term definitions)

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  Cis Peptide Bonds
    Gly A:95 - Gly A:96   [ RasMol ]  
 

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  4p68
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 Related Entries

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

UniProtKB/Swiss-Prot
        C3TR70_ECOLX | C3TR70: 5e8q 5eaj
UniProtKB/TrEMBL
        C3TR70_ECOLX | C3TR70: 4p66

(-) Related Entries Specified in the PDB File

4p66 4P66 CONTAINS THE SAME PROTEIN WITH THE NITRILE PROBE INSTALLED AT A DIFFERENT POSITION