Structure of PDB 1c2t Chain B Binding Site BS01

Receptor Information
>1c2t Chain B (length=209) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVIL
QAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
Ligand information
Ligand IDNHS
InChIInChI=1S/C23H22N4O8/c24-23-26-16-6-1-11(10-15(16)20(31)27-23)9-14(21(32)33)12-2-4-13(5-3-12)19(30)25-17(22(34)35)7-8-18(28)29/h1-6,10,14,17H,7-9H2,(H,25,30)(H,28,29)(H,32,33)(H,34,35)(H3,24,26,27,31)/t14-,17-/m0/s1
InChIKeyDAOQLLQRJAXMGY-YOEHRIQHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC1=Nc2ccc(C[C@H](C(O)=O)c3ccc(cc3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)cc2C(=O)N1
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)C(C(=O)O)Cc3ccc2N=C(NC(=O)c2c3)N)CCC(=O)O
OpenEye OEToolkits 1.5.0c1cc(ccc1C(Cc2ccc3c(c2)C(=O)NC(=N3)N)C(=O)O)C(=O)NC(CCC(=O)O)C(=O)O
CACTVS 3.341NC1=Nc2ccc(C[CH](C(O)=O)c3ccc(cc3)C(=O)N[CH](CCC(O)=O)C(O)=O)cc2C(=O)N1
OpenEye OEToolkits 1.5.0c1cc(ccc1[C@H](Cc2ccc3c(c2)C(=O)NC(=N3)N)C(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)O
FormulaC23 H22 N4 O8
Name10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID
ChEMBL
DrugBankDB02540
ZINCZINC000003870536
PDB chain1c2t Chain B Residue 220 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1c2t New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		R64 F88 M89 R90 I91 L92 N106 H108 L118 V139 T140 D141 L143 D144
Binding residue
(residue number reindexed from 1)		R64 F88 M89 R90 I91 L92 N106 H108 L118 V139 T140 D141 L143 D144
Annotation score2
Binding affinityMOAD: Ki=260nM
PDBbind-CN: -logKd/Ki=6.59,Ki=260nM
Enzymatic activity
Catalytic site (original residue number in PDB) N106 H108 S135 D144
Catalytic site (residue number reindexed from 1) N106 H108 S135 D144
Enzyme Commision number 2.1.2.2: phosphoribosylglycinamide formyltransferase 1.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004644 phosphoribosylglycinamide formyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0006974 DNA damage response
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1c2t, PDBe:1c2t, PDBj:1c2t
PDBsum1c2t
PubMed10606510
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

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