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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | CYS99 |
| A | HIS226 |
| A | HIS230 |
| A | HIS236 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HIS175 |
| A | ASP177 |
| A | HIS190 |
| A | HIS203 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | GLY183 |
| A | ASP185 |
| A | LEU187 |
| A | ASP205 |
| A | GLU208 |
| A | ASP182 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 304 |
| Chain | Residue |
| A | ASP165 |
| A | GLY197 |
| A | GLN199 |
| A | ASP201 |
| A | HOH417 |
| A | HOH460 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 305 |
| Chain | Residue |
| A | ASP131 |
| A | ASP206 |
| A | GLU208 |
| A | HOH450 |
| B | HOH510 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 306 |
| Chain | Residue |
| A | TRP116 |
| A | HIS117 |
| A | HIS118 |
| A | HOH438 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | CYS99 |
| B | HIS226 |
| B | HIS230 |
| B | HIS236 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | HIS175 |
| B | ASP177 |
| B | HIS190 |
| B | HIS203 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 303 |
| Chain | Residue |
| B | ASP182 |
| B | GLY183 |
| B | ASP185 |
| B | LEU187 |
| B | ASP205 |
| B | GLU208 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 304 |
| Chain | Residue |
| B | ASP165 |
| B | GLY197 |
| B | GLN199 |
| B | ASP201 |
| B | HOH420 |
| B | HOH435 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 305 |
| Chain | Residue |
| B | TRP116 |
| B | HIS117 |
| B | HIS118 |
| B | HOH414 |
| B | HOH424 |
| B | HOH493 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 306 |
| Chain | Residue |
| A | GLY105 |
| A | ARG106 |
| A | HOH512 |
| B | SER211 |
| B | GLY215 |
| B | GLN216 |
| B | GLY217 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue 5XQ B 307 |
| Chain | Residue |
| B | VAL101 |
| B | ARG106 |
| B | PHE110 |
| B | LEU114 |
| B | TYR179 |
| B | HIS190 |
| B | ALA191 |
| B | PHE192 |
| B | PRO193 |
| B | HIS230 |
| B | GLY233 |
| B | LEU234 |
| B | HOH479 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL |
| Chain | Residue | Details |
| A | VAL223-LEU232 | |
| site_id | PS00546 |
| Number of Residues | 8 |
| Details | CYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDL |
| Chain | Residue | Details |
| A | PRO97-LEU104 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Motif: {"description":"Cysteine switch","evidences":[{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000303"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in inhibited form","evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by MMP3","evidences":[{"source":"PubMed","id":"1371271","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
