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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 771 |
Chain | Residue |
A | HIS607 |
A | HIS611 |
A | GLU667 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 5HD A 816 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE RDF A 817 |
Chain | Residue |
A | GLU608 |
A | HIS611 |
A | GLU667 |
A | PRO731 |
A | HIS732 |
A | ARG738 |
A | HOH917 |
A | PHE149 |
A | ASN566 |
A | ALA567 |
A | ILE582 |
A | HIS607 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVGHELTHAF |
Chain | Residue | Details |
A | VAL604-PHE613 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU608 | |
Chain | Residue | Details |
A | ASP671 | |
Chain | Residue | Details |
A | HIS607 | |
A | HIS611 | |
A | GLU667 | |
Chain | Residue | Details |
A | ASN166 | |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN187 | |
A | ASN539 | |
A | ASN632 | |
A | ASN651 | |
Chain | Residue | Details |
A | ASN210 | |
Chain | Residue | Details |
A | ASN270 | |
A | ASN316 | |
Chain | Residue | Details |
A | ASN362 | |
A | ASN383 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1r1j |
Chain | Residue | Details |
A | GLU608 | |
A | ASP671 | |
A | HIS732 | |
A | ARG738 | |