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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS93 |
A | HIS97 |
A | HIS103 |
A | E7D303 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | HOH454 |
A | ACE-1 |
A | GLU104 |
A | GLN192 |
A | HOH416 |
A | HOH437 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue E7D A 303 |
Chain | Residue |
A | GLY64 |
A | CYS66 |
A | SER67 |
A | TYR68 |
A | VAL69 |
A | HIS93 |
A | GLU94 |
A | HIS97 |
A | TRP102 |
A | HIS103 |
A | PRO123 |
A | ARG159 |
A | LEU163 |
A | ZN301 |
A | HOH405 |
A | HOH412 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. IVVHELGHVV |
Chain | Residue | Details |
A | ILE90-VAL99 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18824173","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |