Structure of PDB 1gar Chain A Binding Site BS01

Receptor Information
>1gar Chain A (length=204) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHNGDEEHGTSVHFVTDELDGGPVILQAKVP
VFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPP
QGYA
Ligand information
Ligand IDU89
InChIInChI=1S/C27H38N7O12PS/c28-23-18(25(40)33-27(29)32-23)4-3-12-34(21(36)15-48-14-20(35)30-11-1-2-13-46-47(43,44)45)17-7-5-16(6-8-17)24(39)31-19(26(41)42)9-10-22(37)38/h5-8,19H,1-4,9-15H2,(H,30,35)(H,31,39)(H,37,38)(H,41,42)(H2,43,44,45)(H5,28,29,32,33,40)/t19-/m0/s1
InChIKeyWIBNWPBCQGWSJV-IBGZPJMESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1C(=O)NC(CCC(=O)O)C(=O)O)N(CCCC2=C(N=C(NC2=O)N)N)C(=O)CSCC(=O)NCCCCOP(=O)(O)O
CACTVS 3.341NC1=NC(=C(CCCN(C(=O)CSCC(=O)NCCCCO[P](O)(O)=O)c2ccc(cc2)C(=O)N[C@@H](CCC(O)=O)C(O)=O)C(=O)N1)N
OpenEye OEToolkits 1.5.0c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)N(CCCC2=C(N=C(NC2=O)N)N)C(=O)CSCC(=O)NCCCCOP(=O)(O)O
ACDLabs 10.04O=C1C(=C(N=C(N)N1)N)CCCN(c2ccc(C(=O)NC(C(=O)O)CCC(=O)O)cc2)C(=O)CSCC(=O)NCCCCOP(=O)(O)O
CACTVS 3.341NC1=NC(=C(CCCN(C(=O)CSCC(=O)NCCCCO[P](O)(O)=O)c2ccc(cc2)C(=O)N[CH](CCC(O)=O)C(O)=O)C(=O)N1)N
FormulaC27 H38 N7 O12 P S
NameN-[4-[[3-(2,4-DIAMINO-1,6-DIHYDRO-6-OXO-4-PYRIMIDINYL)-PROPYL]-[2-((2-OXO-2-((4-PHOSPHORIBOXY)-BUTYL)-AMINO)-ETHYL)-THIO-ACETYL]-AMINO]BENZOYL]-1-GLUTAMIC ACID
ChEMBL
DrugBank
ZINCZINC000040331395
PDB chain1gar Chain A Residue 213 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1gar Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 A resolution.
Resolution1.96 Å
Binding residue
(original residue number in PDB)		N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 I107 H108 P109 L143 D144 E173
Binding residue
(residue number reindexed from 1)		N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 I107 H108 P109 L138 D139 E168
Annotation score1
Binding affinityMOAD: Ki=100pM
PDBbind-CN: -logKd/Ki=10.00,Ki=100pM
Enzymatic activity
Catalytic site (original residue number in PDB) N106 H108 S135 D144
Catalytic site (residue number reindexed from 1) N106 H108 S130 D139
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1gar, PDBe:1gar, PDBj:1gar
PDBsum1gar
PubMed7776369
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

[Back to BioLiP]