2E2D
Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0031012 | cellular_component | extracellular matrix |
C | 0004857 | molecular_function | enzyme inhibitor activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0008191 | molecular_function | metalloendopeptidase inhibitor activity |
C | 0009725 | biological_process | response to hormone |
C | 0030414 | molecular_function | peptidase inhibitor activity |
C | 0031012 | cellular_component | extracellular matrix |
C | 0034097 | biological_process | response to cytokine |
C | 0046872 | molecular_function | metal ion binding |
C | 0051045 | biological_process | negative regulation of membrane protein ectodomain proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 500 |
Chain | Residue |
A | HIS222 |
A | HIS226 |
A | HIS232 |
C | CYS1001 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | HIS172 |
A | ASP174 |
A | HIS187 |
A | HIS200 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 502 |
Chain | Residue |
A | GLY180 |
A | SER182 |
A | LEU184 |
A | ASP202 |
A | GLU205 |
A | ASP179 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 503 |
Chain | Residue |
A | ASP162 |
A | ASN194 |
A | GLY196 |
A | ASP198 |
A | HOH537 |
A | HOH551 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL |
Chain | Residue | Details |
A | VAL219-LEU228 |
site_id | PS00288 |
Number of Residues | 13 |
Details | TIMP Tissue inhibitors of metalloproteinases signature. CsCsPvHPQqaFC |
Chain | Residue | Details |
C | CYS1001-CYS1013 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 70 |
Details | Region: {"description":"Interaction with TIMP2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8969305","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10926524","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10986126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15734645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780611","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17623656","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19422229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20005097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20726512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22689580","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23810497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23913860","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8576151","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 125 |
Details | Domain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Region: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Site: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"17196980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E2D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hfs |
Chain | Residue | Details |
A | GLU223 | |
A | MET240 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1hfs |
Chain | Residue | Details |
A | GLU223 |