Structure of PDB 1c3e Chain B Binding Site BS02

Receptor Information
>1c3e 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 IDGAR
InChIInChI=1S/C7H15N2O8P/c8-1-4(10)9-7-6(12)5(11)3(17-7)2-16-18(13,14)15/h3,5-7,11-12H,1-2,8H2,(H,9,10)(H2,13,14,15)/p-2/t3-,5-,6-,7-/m1/s1
InChIKeyOBQMLSFOUZUIOB-SHUUEZRQSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@H]([C@@H](O1)NC(=O)CN)O)O)OP(=O)([O-])[O-]
ACDLabs 10.04O=C(NC1OC(C(O)C1O)COP([O-])([O-])=O)CN
CACTVS 3.341NCC(=O)N[CH]1O[CH](CO[P]([O-])([O-])=O)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)NC(=O)CN)O)O)OP(=O)([O-])[O-]
CACTVS 3.341NCC(=O)N[C@@H]1O[C@H](CO[P]([O-])([O-])=O)[C@@H](O)[C@H]1O
FormulaC7 H13 N2 O8 P
NameGLYCINAMIDE RIBONUCLEOTIDE
ChEMBL
DrugBank
ZINC
PDB chain1c3e Chain B Residue 223 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1c3e 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)		G11 S12 N13 G87 F88 M89 P109 E173
Binding residue
(residue number reindexed from 1)		G11 S12 N13 G87 F88 M89 P109 E173
Annotation score5
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:1c3e, PDBe:1c3e, PDBj:1c3e
PDBsum1c3e
PubMed10606510
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

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