Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004176 | molecular_function | ATP-dependent peptidase activity |
E | 0004222 | molecular_function | metalloendopeptidase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006508 | biological_process | proteolysis |
E | 0016020 | cellular_component | membrane |
E | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0004176 | molecular_function | ATP-dependent peptidase activity |
F | 0004222 | molecular_function | metalloendopeptidase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006508 | biological_process | proteolysis |
F | 0016020 | cellular_component | membrane |
F | 0016887 | molecular_function | ATP hydrolysis activity |
G | 0004176 | molecular_function | ATP-dependent peptidase activity |
G | 0004222 | molecular_function | metalloendopeptidase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006508 | biological_process | proteolysis |
G | 0016020 | cellular_component | membrane |
G | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 996 |
Chain | Residue |
E | HIS423 |
E | HIS427 |
E | ASP500 |
E | NHX998 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NHX E 998 |
Chain | Residue |
E | GLY454 |
E | TYR465 |
E | LEU466 |
E | SER495 |
E | GLY496 |
E | ALA498 |
E | ASP500 |
E | ZN996 |
E | HIS423 |
E | GLU424 |
E | HIS427 |
E | LYS451 |
E | LEU453 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 996 |
Chain | Residue |
F | HIS423 |
F | HIS427 |
F | ASP500 |
F | NHX998 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NHX F 998 |
Chain | Residue |
F | HIS423 |
F | GLU424 |
F | HIS427 |
F | LYS451 |
F | ALA452 |
F | LEU453 |
F | SER495 |
F | GLY496 |
F | ALA498 |
F | ASP500 |
F | ZN996 |
G | TYR465 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN G 996 |
Chain | Residue |
G | HIS423 |
G | HIS427 |
G | ASP500 |
G | NHX998 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NHX G 998 |
Chain | Residue |
F | TYR465 |
G | ILE420 |
G | HIS423 |
G | GLU424 |
G | HIS427 |
G | TYR450 |
G | LYS451 |
G | ALA452 |
G | LEU453 |
G | GLY454 |
G | GLY496 |
G | ASN499 |
G | ASP500 |
G | ZN996 |
Functional Information from PROSITE/UniProt
site_id | PS00674 |
Number of Residues | 19 |
Details | AAA AAA-protein family signature. IiVMaATNrpdiLDpALl.R |
Chain | Residue | Details |
E | ILE300-ARG318 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
E | GLU424 | |
F | GLU424 | |
G | GLU424 | |
Chain | Residue | Details |
E | GLY164 | |
F | GLY204 | |
F | LEU209 | |
F | HIS343 | |
F | GLU371 | |
F | HIS423 | |
F | HIS427 | |
F | ASP500 | |
G | GLY164 | |
G | GLY204 | |
G | LEU209 | |
E | GLY204 | |
G | HIS343 | |
G | GLU371 | |
G | HIS423 | |
G | HIS427 | |
G | ASP500 | |
E | LEU209 | |
E | HIS343 | |
E | GLU371 | |
E | HIS423 | |
E | HIS427 | |
E | ASP500 | |
F | GLY164 | |