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3MAT

E.COLI METHIONINE AMINOPEPTIDASE TRANSITION-STATE INHIBITOR COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008198molecular_functionferrous iron binding
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase 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
AGLU204
AGLU235
ACO402
IAHH1
AASP108
AHIS171

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AASP97
AASP108
AGLU235
ACO401
IAHH1

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
ASER72
AASN74
AVAL76
ASER231
AHOH521

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR CHAIN I OF BESTATIN-BASED INHIBITOR (3R)-AMINO-(2S)-HYDROXYHEPTANOYL-L-ALA-L-LEU-L-VAL-L-PHE-OME
ChainResidue
AHIS63
AHIS79
AASP97
ATHR99
AASP108
ATYR168
ACYS169
AHIS171
APHE177
AHIS178
AGLU204
AGLU235
ACO401
ACO402
IHOH7
IHOH76

site_idACT
Number of Residues7
DetailsDINUCLEAR METAL CENTER
ChainResidue
AASP97
AASP108
AHIS171
AGLU204
AGLU235
ACO401
ACO402

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. HDEL
ChainResidueDetails
AHIS262-LEU265

site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGqgfHeepqVl.HY
ChainResidueDetails
ATYR168-TYR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10387007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18093325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18785729","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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 2025-12-24

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