Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0005524 | molecular_function | ATP binding |
B | 0006457 | biological_process | protein folding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0051082 | molecular_function | unfolded protein binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
C | 0005524 | molecular_function | ATP binding |
C | 0006457 | biological_process | protein folding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0051082 | molecular_function | unfolded protein binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
D | 0005524 | molecular_function | ATP binding |
D | 0006457 | biological_process | protein folding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0051082 | molecular_function | unfolded protein binding |
D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
E | 0005524 | molecular_function | ATP binding |
E | 0006457 | biological_process | protein folding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0051082 | molecular_function | unfolded protein binding |
E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
F | 0005524 | molecular_function | ATP binding |
F | 0006457 | biological_process | protein folding |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0051082 | molecular_function | unfolded protein binding |
F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | ARG510 |
A | LYS513 |
A | HIS514 |
A | GLU557 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 3 |
Chain | Residue |
B | ARG510 |
B | LYS513 |
B | HIS514 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 5 |
Chain | Residue |
C | HIS514 |
C | ARG510 |
C | LYS513 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 4 |
Chain | Residue |
D | ARG510 |
D | LYS513 |
D | HIS514 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 E 6 |
Chain | Residue |
E | ARG510 |
E | HIS514 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 1 |
Chain | Residue |
F | ARG510 |
F | LYS513 |
F | HIS514 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG400 | |
B | ARG400 | |
C | ARG400 | |
D | ARG400 | |
E | ARG400 | |
F | ARG400 | |
Chain | Residue | Details |
A | TYR313 | |
E | TYR492 | |
F | TYR313 | |
F | TYR492 | |
A | TYR492 | |
B | TYR313 | |
B | TYR492 | |
C | TYR313 | |
C | TYR492 | |
D | TYR313 | |
D | TYR492 | |
E | TYR313 | |
Chain | Residue | Details |
A | LYS443 | |
C | LYS458 | |
C | LYS489 | |
C | LYS585 | |
D | LYS443 | |
D | LYS458 | |
D | LYS489 | |
D | LYS585 | |
E | LYS443 | |
E | LYS458 | |
E | LYS489 | |
A | LYS458 | |
E | LYS585 | |
F | LYS443 | |
F | LYS458 | |
F | LYS489 | |
F | LYS585 | |
A | LYS489 | |
A | LYS585 | |
B | LYS443 | |
B | LYS458 | |
B | LYS489 | |
B | LYS585 | |
C | LYS443 | |
Chain | Residue | Details |
A | SER453 | |
B | SER453 | |
C | SER453 | |
D | SER453 | |
E | SER453 | |
F | SER453 | |
Chain | Residue | Details |
A | SER476 | |
E | SER641 | |
F | SER476 | |
F | SER641 | |
A | SER641 | |
B | SER476 | |
B | SER641 | |
C | SER476 | |
C | SER641 | |
D | SER476 | |
D | SER641 | |
E | SER476 | |
Chain | Residue | Details |
A | CYS598 | |
B | CYS598 | |
C | CYS598 | |
D | CYS598 | |
E | CYS598 | |
F | CYS598 | |