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2P99

E. coli methionine aminopeptidase monometalated with inhibitor YE6

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008198molecular_functionferrous iron binding
A0008235molecular_functionmetalloexopeptidase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGrgfHeepqVl.HY
ChainResidueDetails
ATYR168-TYR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
AHIS178
AHIS79

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729
ChainResidueDetails
AGLU204
AGLU235
AASP97
AASP108
AHIS171

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228
ChainResidueDetails
ATHR99

221051

PDB entries from 2024-06-12

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