5LYX

CRYSTAL STRUCTURE OF HUMAN METHIONINE AMINOPEPTIDASE-2 IN COMPLEX; WITH AN INHIBITOR 5-((R)-1-[1,2,4]Triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue 7BF A 501

Chain	Residue
A	PHE219
A	MN503
A	HIS231
A	ASP251
A	ASP262
A	HIS331
A	ILE338
A	HIS382
A	TYR444
A	MN502

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site_id	AC2
Number of Residues	6
Details	binding site for residue MN A 502

Chain	Residue
A	ASP262
A	HIS331
A	GLU364
A	GLU459
A	7BF501
A	MN503

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site_id	AC3
Number of Residues	5
Details	binding site for residue MN A 503

Chain	Residue
A	ASP251
A	ASP262
A	GLU459
A	7BF501
A	MN502

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03175","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16540317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	5
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

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