Structure of PDB 2evc Chain A Binding Site BS03

Receptor Information
>2evc Chain A (length=259) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQ
HAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKD
GFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAI
QKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTI
EPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKD
DTIPAIISH
Ligand information
Ligand IDFC3
InChIInChI=1S/C12H7F3O3/c13-12(14,15)8-4-2-1-3-7(8)9-5-6-10(18-9)11(16)17/h1-6H,(H,16,17)
InChIKeyIJPNRBZMRINMMR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(c(c1)c2ccc(o2)C(=O)O)C(F)(F)F
ACDLabs 10.04O=C(O)c2oc(c1c(cccc1)C(F)(F)F)cc2
CACTVS 3.341OC(=O)c1oc(cc1)c2ccccc2C(F)(F)F
FormulaC12 H7 F3 O3
Name5-[2-(TRIFLUOROMETHYL)PHENYL]-2-FUROIC ACID
ChEMBLCHEMBL200377
DrugBankDB07759
ZINCZINC000000349812
PDB chain2evc Chain A Residue 999 [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]
PDB2evc Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		C59 Y62 H63 Y65 C70 H79 D97 D108 H171 H178 E204 W221 E235
Binding residue
(residue number reindexed from 1)		C56 Y59 H60 Y62 C67 H76 D94 D105 H168 H175 E201 W218 E232
Annotation score1
Binding affinityMOAD: ic50=0.29uM
PDBbind-CN: -logKd/Ki=6.54,IC50=0.29uM
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) H76 D94 D105 H168 R172 H175 Q179 E201 N205 Q230 E232
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2evc, PDBe:2evc, PDBj:2evc
PDBsum2evc
PubMed16552144
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

[Back to BioLiP]