Structure of PDB 2gu5 Chain A

Receptor sequence

>2gu5A (length=261) Species: 562 (Escherichia coli)

SIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQ
HAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKD
GFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAI
QKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTI
EPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKD
DTIPAIISHDE

3D structure

• PDB: 2gu5 Structural basis of catalysis by monometalated methionine aminopeptidase.
• Chain: A
• Resolution: 1.6 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	D108 H171 E204 E235	D105 H168 E201 E232
BS02	MN	A	D97 D108 E235	D94 D105 E232
BS03	NLP	A	Y65 H79 D97 D108 F177 H178 E204 E235	Y62 H76 D94 D105 F174 H175 E201 E232

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:2gu5, PDBe:2gu5, PDBj:2gu5
• PDBsum: 2gu5
• PubMed: 16769889
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)