Structure of PDB 2q96 Chain A Binding Site BS03

Receptor Information
>2q96 Chain A (length=263) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDE
Ligand information
Ligand IDA18
InChIInChI=1S/C12H9ClO3/c13-10-4-2-1-3-8(10)7-9-5-6-11(16-9)12(14)15/h1-6H,7H2,(H,14,15)
InChIKeyYRUPEIZURHOLHV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04Clc1ccccc1Cc2oc(cc2)C(=O)O
CACTVS 3.341OC(=O)c1oc(Cc2ccccc2Cl)cc1
OpenEye OEToolkits 1.5.0c1ccc(c(c1)Cc2ccc(o2)C(=O)O)Cl
FormulaC12 H9 Cl O3
Name5-(2-CHLOROBENZYL)-2-FUROIC ACID
ChEMBLCHEMBL197550
DrugBankDB07308
ZINCZINC000016052425
PDB chain2q96 Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2q96 Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		C59 Y62 Y65 H79 D97 D108 H171 H178 E204 W221 E235
Binding residue
(residue number reindexed from 1)		C58 Y61 Y64 H78 D96 D107 H170 H177 E203 W220 E234
Annotation score1
Binding affinityMOAD: ic50=1.2uM
PDBbind-CN: -logKd/Ki=5.92,IC50=1.2uM
BindingDB: IC50=158000nM
Enzymatic activity
Catalytic site (original residue number in PDB) H79 D97 D108 H171 R175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1) H78 D96 D107 H170 R174 H177 Q181 E203 N207 Q232 E234
Enzyme Commision number 3.4.11.18: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008198 ferrous iron binding
GO:0008235 metalloexopeptidase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
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:2q96, PDBe:2q96, PDBj:2q96
PDBsum2q96
PubMed18093325
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

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