Het-PDB Navi2 (PDB: 1B6A)

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Ligands
Code	Name		Style	Show	Link
CO	Cobalt (II) ion				PoSSuM
TN4	(1r,2s,3s,4r)-4-hydroxy-2-methoxy-4-methyl-3-[(2r,3r)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]cyclohexyl (chloroacetyl)carbamate				PoSSuM

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Download interaction data: 1B6A

Code :

1B6A PDBj RCSB PDB PDBe

Header :

ANGIOGENESIS INHIBITOR

Title :

HUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH TNP-470

Release Data :

2000-01-13

Compound :

mol_id	molecule	chains
1	METHIONINE AMINOPEPTIDASE	A
	ec: 3.4.11.18 other_details: TNP-470 COVALENTLY LINKED TO HIS 231 NE2

Source :

mol_id	organism_scientific	organism_common	expression_system
1	Homo sapiens (taxid:9606)	Human	Spodoptera frugiperda MNPV (taxid:10455)
	cellular_location: CYTOPLASM expression_system_cell_line: SF21 expression_system_vector: BACULOVIRUS PACSG2

Authors :

Liu, S., Clardy, J.C.

Keywords :

ANGIOGENESIS INHIBITOR, AMINOPEPTIDASE

Exp. method :

X-RAY DIFFRACTION ( 1.60 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: 1B6A