Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| A | 0016020 | cellular_component | membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008241 | molecular_function | peptidyl-dipeptidase activity |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | HIS367 |
| A | HIS371 |
| A | GLU395 |
| A | X8Z801 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 702 |
| Chain | Residue |
| B | HIS367 |
| B | HIS371 |
| B | GLU395 |
| B | X8Z802 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE X8Z A 801 |
| Chain | Residue |
| A | HIS337 |
| A | ALA338 |
| A | HIS367 |
| A | GLU368 |
| A | HIS371 |
| A | GLU395 |
| A | LYS495 |
| A | HIS497 |
| A | TYR504 |
| A | TYR507 |
| A | ZN701 |
| A | GLN265 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE X8Z B 802 |
| Chain | Residue |
| B | GLN265 |
| B | HIS337 |
| B | ALA338 |
| B | HIS367 |
| B | GLU368 |
| B | HIS371 |
| B | GLU395 |
| B | LYS495 |
| B | HIS497 |
| B | TYR504 |
| B | TYR507 |
| B | ZN702 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVHHELGHIQ |
| Chain | Residue | Details |
| A | THR364-GLN373 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8761461","evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| A | GLU395 | |
| A | TYR507 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| B | GLU395 | |
| B | TYR507 | |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| A | ALA338 | |
| A | GLU368 | |
| A | HIS337 | |
| A | TYR507 | |
| A | HIS497 | |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1i1i |
| Chain | Residue | Details |
| B | ALA338 | |
| B | GLU368 | |
| B | HIS337 | |
| B | TYR507 | |
| B | HIS497 | |
