Brand  (β version)

PDB ID: 5D6E

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Ligands
Code Name Style Show Link
94A (4r,7s)-7-hydroxy-1-(4-methoxybenzyl)-7-methyl-4,5,6,7-tetrahydro-1h-benzotriazol-4-yl propan-2-ylcarbamate PoSSuM
CO Cobalt (II) ion PoSSuM
TBU Tertiary-butyl alcohol PoSSuM
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Structure summary

Code : 5D6E   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structure of human methionine aminopeptidase 2 with covalent spiroepoxytriazole inhibitor (-)-31b
Release Data : 2016-01-13
Compound :
mol_id molecule chains synonym
1 Methionine aminopeptidase 2 A MetAP 2,Initiation factor 2-associated 67 kDa glycoprotein,p67eIF2,Peptidase M
ec: 3.4.11.18
fragment: UNP residues 108-478
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: METAP2, MNPEP, P67EIF2
expression_system_common: Fall armyworm
expression_system_vector_type: baculovirus
Authors : Janowski, R., Miller, A.K., Niessing, D.
Keywords : Methionine aminopeptidase 2, Spiroepoxytriazoles, inhibitor, hydrolase
Exp. method : X-RAY DIFFRACTION ( 1.49 Å )
Citation :

Spiroepoxytriazoles Are Fumagillin-like Irreversible Inhibitors of MetAP2 with Potent Cellular Activity.

Morgen, M.,Jost, C.,Malz, M.  et al.
(2016)  Acs Chem.Biol.  11 : 1001 - 1011

PubMed: 26686773
DOI: 10.1021/acschembio.5b00755

Reaction

Chain : A
UniProt : P50579 (MAP2_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. 3.4.11.18 HAMAP-Rule:MF_03175, PubMed:20521764
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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.