Brand  (β version)

PDB ID: 1B59

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CO Cobalt (II) ion PoSSuM
OVA 3,4-dihydroxy-2-methoxy-4-methyl-3-[2-methyl-3-(3-methyl-but-2-enyl) -oxiranyl]-cyclohexanone PoSSuM

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Glycosylation
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Structure summary

Code : 1B59   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : COMPLEX OF HUMAN METHIONINE AMINOPEPTIDASE-2 COMPLEXED WITH OVALICIN
Release Data : 2000-01-14
Compound :
mol_id molecule chains synonym
1 PROTEIN (METHIONINE AMINOPEPTIDASE) A METAP 2
ec: 3.4.11.18
other_details: OVALICIN 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_strain: SF21
expression_system_cell_line: SF21
expression_system_vector_type: VIRUS
expression_system_vector: BACULOVIRUS
other_details: PROTEIN WAS EXPRESSED IN SF21 INSECT CELLS.. BACULOVIRUS PACSG2 VECTOR
Authors : Liu, S., Clardy, J.C.
Keywords : ANGIOGENESIS INHIBITOR, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.80 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

PubMed: 9812898
DOI: 10.1126/science.282.5392.1324

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
-
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.