Brand  (β version)

PDB ID: 2EVM

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Ligands
Code Name Style Show Link
FC2 5-(2,5-dichlorophenyl)-2-furoic acid PoSSuM
MN Manganese (II) ion PoSSuM
NA Sodium ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2EVM   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : crystal structure of methionine aminopeptidase in complex with 5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Release Data : 2006-03-28
Compound :
mol_id molecule chains synonym
1 Methionine aminopeptidase A MAP, Peptidase M
ec: 3.4.11.18
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
expression_system_strain: BL21(DE3)pLysS
expression_system_vector_type: plasmid
expression_system_plasmid: pGEMEX-1
Authors : Huang, W.-J.
Keywords : methionine aminopeptidase, complex, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.7 Å )
Citation :

Structural analysis of metalloform-selective inhibition of methionine aminopeptidase.

Xie, S.X.,Huang, W.J.,Ma, Z.Q.  et al.
(2006)  Acta Crystallogr.,Sect.D  62 : 425 - 432

PubMed: 16552144
DOI: 10.1107/S0907444906003878

Reaction

Chain : A
UniProt : P0AE18 (MAP1_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. 3.4.11.18 HAMAP-Rule:MF_01974, PubMed:17120228, PubMed:20521764, PubMed:3027045
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Cofactor: Evidence: Note:
Fe(2+) ECO:0000255 | HAMAP-Rule:MF_01974
ECO:0000269 | PubMed:10387007
ECO:0000269 | PubMed:10460163
ECO:0000269 | PubMed:10555963
ECO:0000269 | PubMed:10736182
ECO:0000269 | PubMed:17120228
ECO:0000269 | PubMed:20017927
ECO:0000255 | HAMAP-Rule:MF_01974
ECO:0000269 | PubMed:10460163
ECO:0000255 | HAMAP-Rule:MF_01974
ECO:0000269 | PubMed:10460163
ECO:0000269 | PubMed:16769889
ECO:0000269 | PubMed:18093325
ECO:0000255 | HAMAP-Rule:MF_01974
ECO:0000269 | PubMed:10460163
ECO:0000269 | PubMed:10736182
ECO:0000269 | PubMed:18785729
ECO:0000269 | PubMed:22112844
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.
Na(+) ECO:0000269 | PubMed:10387007
Binds 1 sodium ion per subunit. The sodium ion has a structural role.