Structure of PDB 1wkm Chain B

Receptor sequence

>1wkmB (length=295) Species: 2261 (Pyrococcus furiosus)

MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKMIMELGGKPAF
PVNLSINEIAAHYTPYKGDTTVLKEGDYLKIDVGVHIDGFIADTAVTVRV
GMEEDELMEAAKEALNAAISVARAGVEIKELGKAIENEIRKRGFKPIVNL
SGHKIERYKLHAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEV
PPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWLQNDMPEGQLK
LALKTLEKAGAIYGYPVLKEIRNGIVAQFEHTIIVEKDSVIVTTE

3D structure

• PDB: 1wkm EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D82 D93 H153 H161 E187 E280
• Catalytic site (residue number reindexed from 1): D82 D93 H153 H161 E187 E280
• 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	B	D82 D93 E280	D82 D93 E280
BS02	MN	B	D93 H153 E187 E280	D93 H153 E187 E280
BS03	MET	B	F50 N53 H62 D82 D93 H161 E187 I205	F50 N53 H62 D82 D93 H161 E187 I205	MOAD: Ki=150mM

Gene Ontology

Molecular Function

• GO:0004177 aminopeptidase activity
• GO:0004239 initiator methionyl aminopeptidase activity
• GO:0008235 metalloexopeptidase activity
• GO:0046872 metal ion binding
• GO:0070006 metalloaminopeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1wkm, PDBe:1wkm, PDBj:1wkm
• PDBsum: 1wkm
• PubMed: 15628852
• UniProt: P56218|MAP2_PYRFU Methionine aminopeptidase (Gene Name=map)