Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0005524 | molecular_function | ATP binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 701 |
Chain | Residue |
A | GLN513 |
A | ARG517 |
A | HOH973 |
D | PRO16 |
D | ARG17 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 701 |
Chain | Residue |
B | HOH968 |
B | LYS502 |
B | SER504 |
B | HOH827 |
B | HOH967 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 101 |
Chain | Residue |
A | MET404 |
A | GLY405 |
C | PRO11 |
C | ARG12 |
C | HOH204 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR CHAIN C OF APO-MONOMER |
Chain | Residue |
A | ILE401 |
A | GLU402 |
A | THR403 |
A | MET404 |
A | GLN424 |
A | VAL425 |
A | PHE426 |
A | SER427 |
A | THR428 |
A | ALA429 |
A | GLU430 |
A | GLN433 |
A | ARG467 |
A | GLN471 |
A | ASP540 |
A | HOH803 |
C | SO4101 |
C | HOH201 |
C | HOH203 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR CHAIN D OF APO-MONOMER |
Chain | Residue |
A | VAL516 |
A | ARG517 |
A | ASP518 |
A | GLU520 |
A | ALA521 |
A | ASN522 |
A | SO4701 |
B | ILE401 |
B | THR403 |
B | MET404 |
B | GLN424 |
B | VAL425 |
B | PHE426 |
B | SER427 |
B | THR428 |
B | ALA429 |
B | GLN433 |
B | ALA435 |
B | VAL436 |
B | THR437 |
B | ILE438 |
B | ASN458 |
B | GLY468 |
B | MET469 |
B | PRO470 |
B | GLN471 |
B | HOH962 |
D | HOH101 |
D | HOH102 |
D | HOH103 |
D | HOH104 |
D | HOH105 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS421 | |
A | LYS556 | |
B | LYS421 | |
B | LYS556 | |
Chain | Residue | Details |
A | LYS502 | |
A | LYS528 | |
A | LYS587 | |
B | LYS502 | |
B | LYS528 | |
B | LYS587 | |