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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 201 |
Chain | Residue |
A | HIS405 |
A | HIS409 |
A | HIS415 |
A | IH6478 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 202 |
Chain | Residue |
B | HIS405 |
B | HIS409 |
B | HIS415 |
B | IH6478 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE IH6 A 478 |
Chain | Residue |
A | HOH56 |
A | ZN201 |
A | THR347 |
A | LEU348 |
A | GLY349 |
A | LEU350 |
A | LEU401 |
A | VAL402 |
A | HIS405 |
A | GLU406 |
A | HIS409 |
A | HIS415 |
A | VAL434 |
A | PRO437 |
A | VAL440 |
A | HOH16 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE IH6 B 478 |
Chain | Residue |
B | HOH110 |
B | ZN202 |
B | GLU290 |
B | GLY346 |
B | THR347 |
B | LEU348 |
B | GLY349 |
B | GLU398 |
B | LEU401 |
B | HIS405 |
B | GLU406 |
B | HIS409 |
B | HIS415 |
B | VAL434 |
B | ALA439 |
B | VAL440 |
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 | |