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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 257 |
| Chain | Residue |
| A | CYS75 |
| A | HIS201 |
| A | HIS205 |
| A | HIS211 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 258 |
| Chain | Residue |
| A | HIS151 |
| A | ASP153 |
| A | HIS166 |
| A | TYR168 |
| A | HIS179 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 259 |
| Chain | Residue |
| A | ASP158 |
| A | GLY159 |
| A | GLY161 |
| A | VAL163 |
| A | ASP181 |
| A | GLU184 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 260 |
| Chain | Residue |
| A | ASP141 |
| A | GLY173 |
| A | ASN175 |
| A | ASP177 |
| A | HOH306 |
| A | HOH312 |
| site_id | CA1 |
| Number of Residues | 6 |
| Details | CA1 ARE THE LIGANDS OF THE CALCIUM ION CA 259 |
| Chain | Residue |
| A | GLY159 |
| A | GLY161 |
| A | VAL163 |
| A | ASP181 |
| A | GLU184 |
| A | ASP158 |
| site_id | CA2 |
| Number of Residues | 6 |
| Details | CA2 ARE THE LIGANDS OF THE CALCIUM ION CA 260 |
| Chain | Residue |
| A | ASP141 |
| A | GLY173 |
| A | ASN175 |
| A | ASP177 |
| A | HOH306 |
| A | HOH312 |
| site_id | ZN1 |
| Number of Residues | 4 |
| Details | ZN1 ARE THE LIGANDS OF THE CATALYTIC (ZN 257) ZINC ION. |
| Chain | Residue |
| A | CYS75 |
| A | HIS201 |
| A | HIS205 |
| A | HIS211 |
| site_id | ZN2 |
| Number of Residues | 4 |
| Details | ZN2 ARE THE LIGANDS OF THE STRUCTURAL (ZN 258) ZINC ION. |
| Chain | Residue |
| A | HIS151 |
| A | ASP153 |
| A | HIS166 |
| A | HIS179 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEIGHSL |
| Chain | Residue | Details |
| A | VAL198-LEU207 | |
| site_id | PS00546 |
| Number of Residues | 8 |
| Details | CYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDV |
| Chain | Residue | Details |
| A | PRO73-VAL80 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Motif: {"description":"Cysteine switch","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"in inhibited form"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8740360","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | |
| Chain | Residue | Details |
| A | GLU202 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 591 |
| Chain | Residue | Details |
| A | HIS201 | metal ligand |
| A | GLU202 | proton acceptor, proton donor |
| A | HIS205 | metal ligand |
| A | HIS211 | metal ligand |
