8OXG

Crystal structure of human methionine aminopeptidase-2 complexed with (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-2-buten-1-yl)-2-oxiranyl]-1-oxaspiro[2.5]oct-6-yl N-(trans-4-aminocyclohexyl)carbamate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0070006	molecular_function	metalloaminopeptidase activity
B	0006508	biological_process	proteolysis
B	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PROSITE/UniProt

site_id	PS01202
Number of Residues	17
Details	MAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD

Chain	Residue	Details
A	ASP246-ASP262

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16540317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16134930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16540317","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17350258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17636946","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---