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 |
B | 0004222 | molecular_function | metalloendopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | INN3 |
A | HIS405 |
A | HIS409 |
A | HIS415 |
A | HOH661 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 4 |
Chain | Residue |
B | HOH642 |
B | INN2 |
B | HIS405 |
B | HIS409 |
B | HIS415 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 475 |
Chain | Residue |
A | ASP342 |
A | PHE343 |
A | ASN389 |
A | HOH659 |
A | HOH660 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE INN B 2 |
Chain | Residue |
B | ZN4 |
B | MET345 |
B | GLY346 |
B | THR347 |
B | LEU348 |
B | GLY349 |
B | ASN389 |
B | HIS405 |
B | GLU406 |
B | HIS409 |
B | HIS415 |
B | PRO437 |
B | ILE438 |
B | ALA439 |
B | HOH630 |
B | HOH642 |
B | HOH645 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE INN A 3 |
Chain | Residue |
A | ZN1 |
A | GLU327 |
A | SER330 |
A | MET345 |
A | GLY346 |
A | THR347 |
A | LEU348 |
A | GLY349 |
A | ASN389 |
A | TYR390 |
A | HIS405 |
A | GLU406 |
A | HIS409 |
A | HIS415 |
A | PRO437 |
A | ILE438 |
A | ALA439 |
A | HOH642 |
A | HOH661 |
A | HOH662 |
A | HOH663 |
A | HOH665 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IMD B 475 |
Chain | Residue |
B | ARG357 |
B | ALA358 |
B | ASN359 |
B | CIT500 |
B | HOH589 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT B 500 |
Chain | Residue |
A | PRO356 |
A | HIS415 |
A | PRO437 |
B | ARG357 |
B | ASN359 |
B | SER360 |
B | HIS361 |
B | IMD475 |
B | HOH631 |
B | HOH643 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA B 501 |
Chain | Residue |
A | GLU280 |
B | LEU420 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE IPA A 476 |
Chain | Residue |
A | LEU285 |
A | LYS286 |
A | SER287 |
A | PRO288 |
A | GLN289 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA B 502 |
Chain | Residue |
B | LYS286 |
B | SER287 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA B 503 |
Chain | Residue |
B | ILE279 |
B | GLU280 |
B | HOH646 |
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 | |
B | GLU406 | |
Chain | Residue | Details |
A | HIS405 | |
A | HIS409 | |
A | HIS415 | |
B | HIS405 | |
B | HIS409 | |
B | HIS415 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN264 | |
A | GLN452 | |
B | ASN264 | |
B | GLN452 | |