Structure of PDB 2q95 Chain A

Receptor sequence
>2q95A (length=263) Species: 562 (Escherichia coli) [Search protein sequence]
AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDE
3D structure
PDB2q95 Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A D97 D108 E235 D96 D107 E234
BS02 MN A D108 H171 T202 E204 E235 D107 H170 T201 E203 E234
BS03 A05 A Y62 H63 H79 D97 D108 H171 H178 E204 W221 E235 Y61 H62 H78 D96 D107 H170 H177 E203 W220 E234 MOAD: ic50=1.6uM
PDBbind-CN: -logKd/Ki=5.80,IC50=1.6uM
BindingDB: IC50=48600nM
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:2q95, PDBe:2q95, PDBj:2q95
PDBsum2q95
PubMed18093325
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

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