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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | HIS405 |
A | HIS409 |
A | HIS415 |
A | 440501 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 503 |
Chain | Residue |
A | ASP342 |
A | PHE343 |
A | ASN389 |
A | TYR390 |
A | HOH566 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 440 A 501 |
Chain | Residue |
A | GLY346 |
A | THR347 |
A | LEU348 |
A | GLY349 |
A | GLU398 |
A | LEU401 |
A | HIS405 |
A | GLU406 |
A | HIS415 |
A | PRO437 |
A | ALA439 |
A | VAL440 |
A | ZN502 |
A | HOH524 |
A | HOH676 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF |
Chain | Residue | Details |
A | VAL402-PHE411 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU406 | |
Chain | Residue | Details |
A | HIS405 | |
A | HIS409 | |
A | HIS415 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN264 | |
A | GLN452 | |