Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| C | 0004222 | molecular_function | metalloendopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHGV |
| Chain | Residue | Details |
| A | VAL349-VAL358 | |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CyCedGYardvngk.C |
| Chain | Residue | Details |
| E | CYS63-CYS77 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9753696","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9753696","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BQB","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9738891","evidenceCode":"ECO:0000269"}]} |