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 301 |
| Chain | Residue |
| A | DPS502 |
| A | HIS201 |
| A | HIS205 |
| A | HIS211 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 302 |
| Chain | Residue |
| A | HIS151 |
| A | ASP153 |
| A | HIS166 |
| A | HIS179 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 303 |
| 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 SO4 A 501 |
| Chain | Residue |
| A | PRO109 |
| A | PRO109 |
| A | LYS110 |
| A | LYS110 |
| A | HOH542 |
| A | HOH542 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | ASP141 |
| A | GLY173 |
| A | ASN175 |
| A | ASP177 |
| A | HOH574 |
| A | HOH575 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 305 |
| Chain | Residue |
| A | ASP107 |
| A | ASP182 |
| A | GLU184 |
| A | HOH576 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DPS A 502 |
| Chain | Residue |
| A | LEU164 |
| A | ALA165 |
| A | ALA167 |
| A | HIS201 |
| A | GLU202 |
| A | HIS205 |
| A | PHE210 |
| A | HIS211 |
| A | TYR220 |
| A | PRO221 |
| A | LEU222 |
| A | TYR223 |
| A | HIS224 |
| A | ZN301 |
| A | HOH566 |
| site_id | CA1 |
| Number of Residues | 1 |
| Details | CA1 IS THE FIRST CALCIUM BINDING SITE. |
| site_id | CA2 |
| Number of Residues | 1 |
| Details | CA2 IS THE SECOND CALCIUM BINDING SITE. |
| site_id | CA3 |
| Number of Residues | 1 |
| Details | CA3 IS THE THIRD CALCIUM BINDING SITE. |
| site_id | IN2 |
| Number of Residues | 1 |
| Details | IN2 IS THE BINDING SITE FOR THE DIPHENYLPIPERIDINE SULFONAMIDE INHIBITOR. |
| site_id | ZN1 |
| Number of Residues | 1 |
| Details | ZN1 IS THE CATALYTIC ZINC BINDING SITE. |
| site_id | ZN2 |
| Number of Residues | 1 |
| Details | ZN1 IS THE STRUCTURAL ZINC BINDING SITE. |
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 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1hfs |
| Chain | Residue | Details |
| A | MET219 | |
| A | GLU202 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hfs |
| 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 |
