Structure of PDB 3g31 Chain A Binding Site BS02

Receptor Information
>3g31 Chain A (length=262) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMA
AAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAA
LQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGD
PRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLP
TSWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDV
LASAARIIAEGL
Ligand information
Ligand IDGF1
InChIInChI=1S/C12H15NO4/c1-5(12(16)17)13-10(14)8-6-2-3-7(4-6)9(8)11(13)15/h5-9H,2-4H2,1H3,(H,16,17)/t5-,6-,7+,8-,9+/m0/s1
InChIKeyREFMTLIXGKZVDF-VRGHQRLXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(N2C(=O)C3C1CCC(C1)C3C2=O)C
OpenEye OEToolkits 1.5.0CC(C(=O)O)N1C(=O)C2C3CCC(C3)C2C1=O
OpenEye OEToolkits 1.5.0C[C@@H](C(=O)O)N1C(=O)[C@H]2[C@H]3CC[C@H](C3)[C@H]2C1=O
CACTVS 3.341C[CH](N1C(=O)[CH]2[CH]3CC[CH](C3)[CH]2C1=O)C(O)=O
CACTVS 3.341C[C@H](N1C(=O)[C@H]2[C@H]3CC[C@H](C3)[C@H]2C1=O)C(O)=O
FormulaC12 H15 N O4
Name(2S)-2-[(3aR,4R,7S,7aS)-1,3-dioxooctahydro-2H-4,7-methanoisoindol-2-yl]propanoic acid
ChEMBL
DrugBankDB07823
ZINCZINC000002317458
PDB chain3g31 Chain A Residue 4 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3g31 Molecular docking and ligand specificity in fragment-based inhibitor discovery
Resolution1.7 Å
Binding residue
(original residue number in PDB)		S70 N104 Y105 S130 N132 G236 S237
Binding residue
(residue number reindexed from 1)		S44 N78 Y79 S104 N106 G210 S211
Annotation score1
Binding affinityMOAD: Ki=1.3mM
PDBbind-CN: -logKd/Ki=2.89,Ki=1.3mM
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S44 K47 S104 E140 K208 S211
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3g31, PDBe:3g31, PDBj:3g31
PDBsum3g31
PubMed19305397
UniProtQ9L5C8

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