6HV2
MMP-13 in complex with the peptide IMISF
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS222 |
A | HIS226 |
A | HIS232 |
B | ILE163 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | HIS172 |
A | ASP174 |
A | HIS187 |
A | HIS200 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 303 |
Chain | Residue |
A | GLY180 |
A | SER182 |
A | LEU184 |
A | ASP202 |
A | GLU205 |
A | ASP179 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue CA A 304 |
Chain | Residue |
A | TYR104 |
A | ASP162 |
A | ASN194 |
A | GLY196 |
A | ASP198 |
A | HOH421 |
A | HOH431 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CA A 305 |
Chain | Residue |
A | ASP128 |
A | ASP203 |
A | GLU205 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | ALA188 |
A | HIS226 |
A | HIS232 |
A | HIS232 |
A | LYS234 |
A | HOH472 |
B | ILE163 |
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 | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860 |
Chain | Residue | Details |
A | GLU223 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
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 | |
A | ASP162 | |
A | ASP179 | |
A | GLY180 | |
A | SER182 | |
A | LEU184 | |
A | ASN194 | |
A | GLY196 | |
A | ASP198 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | |
A | ASP174 | |
A | HIS187 | |
A | HIS200 | |
A | HIS222 | |
A | HIS226 | |
A | HIS232 | |
A | MET240 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151 |
Chain | Residue | Details |
A | ASN117 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN152 |