Het-PDB Navi2 (PDB: 2EA2)

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Ligands
Code	Name		Style	Show	Link
F77	3-ethyl-6-{[(4-fluorophenyl)sulfonyl]amino}-2-methylbenzoic acid				PoSSuM
MN	Manganese (II) ion				PoSSuM

Non-standard Residues
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Download interaction data: 2EA2

Code :

2EA2 PDBj RCSB PDB PDBe

Header :

HYDROLASE

Title :

H-MetAP2 complexed with A773812

Release Data :

2008-02-05

Compound :

mol_id	molecule	chains	synonym
1	Methionine aminopeptidase 2	A	MetAP 2, Peptidase M 2, Initiation factor 2-associated 67 kDa glycoprotein, p67, p67eIF2
	ec: 3.4.11.18 fragment: residues 110-478

Source :

mol_id	organism_scientific	organism_common	expression_system
1	Homo sapiens (taxid:9606)	Human	Escherichia coli (taxid:562)
	expression_system_vector_type: plasmid

Authors :

Park, C.H.

Keywords :

Protein-ligand complex, HYDROLASE

Exp. method :

X-RAY DIFFRACTION ( 2.50 Å )

Citation :

Lead optimization of methionine aminopeptidase-2 (MetAP2) inhibitors containing sulfonamides of 5,6-disubstituted anthranilic acids

Wang, G.T.,Mantei, R.A.,Kawai, M. et al.
(2007) Bioorg.Med.Chem.Lett. 17 : 2817 - 2822

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: 2EA2