Het-PDB Navi2 (PDB: 1BOA)

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Ligands
Code	Name		Style	Show	Link
CO	Cobalt (II) ion				PoSSuM
FUG	Fumagillin				PoSSuM

Non-standard Residues
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Glycosylation
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Download interaction data: 1BOA

Code :

1BOA PDBj RCSB PDB PDBe

Header :

AMINOPEPTIDASE

Title :

HUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH ANGIOGENESIS INHIBITOR FUMAGILLIN

Release Data :

1999-08-01

Compound :

mol_id	molecule	chains
1	METHIONINE AMINOPEPTIDASE	A
	ec: 3.4.11.18 other_details: COMPLEX WITH FUMAGILLIN AND COBALT

Source :

mol_id	organism_scientific	organism_common	expression_system
1	Homo sapiens (taxid:9606)	Human	Spodoptera frugiperda (taxid:7108)
	cellular_location: CYTOPLASM expression_system_common: Fall armyworm expression_system_cell_line: SF21 CELLS expression_system_vector: BACULOVIRUS, PACSG2

Authors :

Liu, S., Widom, J., Kemp, C.W., Crews, C.M., Clardy, J.C.

Keywords :

METHIONINE AMINOPEPTIDASE, ANGIOGENESIS INHIBITOR, FUMAGILLIN, HYDROLASE, AMINOPEPTIDASE

Exp. method :

X-RAY DIFFRACTION ( 1.8 Å )

Citation :

Structure of human methionine aminopeptidase-2 complexed with fumagillin.

Liu, S.,Widom, J.,Kemp, C.W. et al.
(1998) Science 282 : 1324 - 1327

Chain :

UniProt :

P50579 (MAP2_HUMAN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	3.4.11.18	HAMAP-Rule:MF_03175, PubMed:20521764
	-	HAMAP-Rule:MF_03175, PubMed:20521764
Cofactor:	Evidence:	Note:
Fe(2+)	ECO:0000255 \| HAMAP-Rule:MF_03175 ECO:0000269 \| PubMed:12718546 ECO:0000269 \| PubMed:17636946 ECO:0000269 \| PubMed:9812898 ECO:0000255 \| HAMAP-Rule:MF_03175 ECO:0000269 \| PubMed:12718546 ECO:0000269 \| PubMed:17636946 ECO:0000269 \| PubMed:9812898 ECO:0000255 \| HAMAP-Rule:MF_03175 ECO:0000269 \| PubMed:12718546 ECO:0000269 \| PubMed:17636946 ECO:0000269 \| PubMed:9812898 ECO:0000255 \| HAMAP-Rule:MF_03175 ECO:0000269 \| PubMed:12718546 ECO:0000269 \| PubMed:17636946 ECO:0000269 \| PubMed:9812898	Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. Also manganese has been proposed to be the physiological cofactor for human METAP2.

PDB ID: 1BOA