7JU8
X-ray structure of MMP-13 in Complex with 4-(1,2,3-thiadiazol-4-yl)pyridine
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 |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0031012 | cellular_component | extracellular matrix |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860 |
Chain | Residue | Details |
A | GLU223 | |
B | GLU223 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305 |
Chain | Residue | Details |
A | ASP128 | |
A | ASP202 | |
A | ASP203 | |
A | GLU205 | |
B | ASP128 | |
B | ASP162 | |
B | ASP179 | |
B | GLY180 | |
B | SER182 | |
B | LEU184 | |
B | ASN194 | |
A | ASP162 | |
B | GLY196 | |
B | ASP198 | |
B | ASP202 | |
B | ASP203 | |
B | GLU205 | |
A | ASP179 | |
A | GLY180 | |
A | SER182 | |
A | LEU184 | |
A | ASN194 | |
A | GLY196 | |
A | ASP198 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860 |
Chain | Residue | Details |
A | HIS172 | |
B | ASP174 | |
B | HIS187 | |
B | HIS200 | |
B | HIS222 | |
B | HIS226 | |
B | HIS232 | |
B | MET240 | |
A | ASP174 | |
A | HIS187 | |
A | HIS200 | |
A | HIS222 | |
A | HIS226 | |
A | HIS232 | |
A | MET240 | |
B | HIS172 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151 |
Chain | Residue | Details |
A | ASN117 | |
B | ASN117 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN152 | |
B | ASN152 |