Structure of PDB 2evm Chain A

Receptor sequence

>2evmA (length=259) Species: 562 (Escherichia coli)

SIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQ
HAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKD
GFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAI
QKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTI
EPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKD
DTIPAIISH

3D structure

• PDB: 2evm Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.
• Chain: A
• Resolution: 1.7 Å

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.

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	D94 D105 E232
BS02	MN	A	D108 H171 T202 E204 E235	D105 H168 T199 E201 E232
BS03	FC2	A	Y62 H63 Y65 C70 H79 D97 D108 H171 H178 E204 W221 E235	Y59 H60 Y62 C67 H76 D94 D105 H168 H175 E201 W218 E232	MOAD: ic50=0.693uM PDBbind-CN: -logKd/Ki=6.16,IC50=0.693uM BindingDB: IC50=84000nM

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

External links

• PDB: RCSB:2evm, PDBe:2evm, PDBj:2evm
• PDBsum: 2evm
• PubMed: 16552144
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)