1MAT
STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004239 | molecular_function | initiator methionyl aminopeptidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO A 401 |
| Chain | Residue |
| A | THR202 |
| A | GLU204 |
| A | GLU235 |
| A | CO402 |
| A | ASP108 |
| A | HIS171 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 402 |
| Chain | Residue |
| A | ASP97 |
| A | ASP108 |
| A | GLU235 |
| A | CO401 |
| site_id | ACT |
| Number of Residues | 7 |
| Details |
| Chain | Residue |
| A | ASP97 |
| A | ASP108 |
| A | HIS171 |
| A | GLU204 |
| A | GLU235 |
| A | CO401 |
| A | ALA2 |
Functional Information from PROSITE/UniProt
| site_id | PS00680 |
| Number of Residues | 19 |
| Details | MAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGrgfHeepqVl.HY |
| Chain | Residue | Details |
| A | TYR168-TYR186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU204 | |
| A | GLN182 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU204 |
