Structure of PDB 3a8i Chain C Binding Site BS01

Receptor Information
>3a8i Chain C (length=363) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AQQTPLYEQHTLCGARMVDFHGWMMPLHYGSQIDEHHAVRTDAGMFDVSH
MTIVDLRGSRTREFLRYLLANDVAKLTKSGKALYSGMLNASGGVIDDLIV
YYFTEDFFRLVVNSATREKDLSWITQHAEPFGIEITVRDDLSMIAVQGPN
AQAKAATLFNDAQRQAVEGMKPFFGVQAGDLFIATTGYTGEAGYEIALPN
EKAADFWRALVEAGVKPCGLGARDTLRLEAGMNLYGQEMDETISPLAANM
GWTIAWEPADRDFIGREALEVQREHGTEKLVGLVMTEKGVLRNELPVRFT
DAQGNQHEGIITSGTFSPTLGYSIALARVPEGIGETAIVQIRNREMPVKV
TKPVFVRNGKAVA
Ligand information
Ligand IDC2F
InChIInChI=1S/C20H25N7O6/c1-27-12(9-23-16-15(27)18(31)26-20(21)25-16)8-22-11-4-2-10(3-5-11)17(30)24-13(19(32)33)6-7-14(28)29/h2-5,12-13,22H,6-9H2,1H3,(H,24,30)(H,28,29)(H,32,33)(H4,21,23,25,26,31)/t12-,13-/m0/s1
InChIKeyZNOVTXRBGFNYRX-STQMWFEESA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN1[CH](CNc2ccc(cc2)C(=O)N[CH](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)NCC2N(C=3C(=O)NC(=NC=3NC2)N)C)CCC(=O)O
OpenEye OEToolkits 1.5.0CN1C(CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)NC(CCC(=O)O)C(=O)O
OpenEye OEToolkits 1.5.0C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341CN1[C@@H](CNc2ccc(cc2)C(=O)N[C@@H](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
FormulaC20 H25 N7 O6
Name5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID
ChEMBLCHEMBL1231574
DrugBankDB11256
ZINCZINC000002005305
PDB chain3a8i Chain C Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3a8i Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism
Resolution1.99 Å
Binding residue
(original residue number in PDB)		M51 Y84 D97 I99 V111 N113 F173 Y188 E195 M232 W252
Binding residue
(residue number reindexed from 1)		M51 Y84 D97 I99 V111 N113 F173 Y188 E195 M232 W252
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) D97
Catalytic site (residue number reindexed from 1) D97
Enzyme Commision number 2.1.2.10: aminomethyltransferase.
Gene Ontology
Molecular Function
GO:0004047 aminomethyltransferase activity
GO:0008483 transaminase activity
Biological Process
GO:0006546 glycine catabolic process
GO:0006730 one-carbon metabolic process
GO:0019464 glycine decarboxylation via glycine cleavage system
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005960 glycine cleavage complex

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3a8i, PDBe:3a8i, PDBj:3a8i
PDBsum3a8i
PubMed20375021
UniProtP27248|GCST_ECOLI Aminomethyltransferase (Gene Name=gcvT)

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