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1MAT

STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME

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
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
ATHR202
AGLU204
AGLU235
ACO402
AASP108
AHIS171

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AASP97
AASP108
AGLU235
ACO401

site_idACT
Number of Residues7
Details
ChainResidue
AASP97
AASP108
AHIS171
AGLU204
AGLU235
ACO401
AALA2

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
AHIS79
AHIS178

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
AASP97
AASP108
AHIS171
AGLU204
AGLU235

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204
AGLN182

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU204

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PDB entries from 2024-07-24

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