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 |
C | 0005524 | molecular_function | ATP binding |
C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
D | 0005524 | molecular_function | ATP binding |
D | 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 MG A 501 |
Chain | Residue |
A | ASP34 |
A | PO4502 |
A | ADP503 |
A | HOH610 |
A | HOH641 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 502 |
Chain | Residue |
A | THR226 |
A | MG501 |
A | ADP503 |
A | HOH602 |
A | HOH641 |
A | GLY36 |
A | THR37 |
A | LYS95 |
A | GLU199 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue ADP A 503 |
Chain | Residue |
A | GLY36 |
A | THR37 |
A | THR38 |
A | TYR39 |
A | GLY223 |
A | GLY224 |
A | GLY252 |
A | GLU253 |
A | GLU290 |
A | LYS293 |
A | ARG294 |
A | SER297 |
A | GLY360 |
A | GLY361 |
A | SER362 |
A | ARG364 |
A | ASP388 |
A | MG501 |
A | PO4502 |
A | HOH602 |
A | HOH610 |
A | HOH628 |
A | HOH635 |
A | HOH637 |
A | HOH646 |
D | HOH691 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 501 |
Chain | Residue |
B | PO4502 |
B | ADP503 |
B | HOH631 |
B | HOH640 |
B | HOH652 |
B | HOH689 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue PO4 B 502 |
Chain | Residue |
B | GLY36 |
B | THR37 |
B | LYS95 |
B | PRO171 |
B | GLU199 |
B | THR226 |
B | MG501 |
B | ADP503 |
B | HOH611 |
B | HOH631 |
B | HOH640 |
B | HOH652 |
B | HOH654 |
site_id | AC6 |
Number of Residues | 26 |
Details | binding site for residue ADP B 503 |
Chain | Residue |
B | GLY36 |
B | THR37 |
B | THR38 |
B | TYR39 |
B | ILE61 |
B | GLY223 |
B | GLY224 |
B | GLU290 |
B | LYS293 |
B | ARG294 |
B | SER297 |
B | GLY360 |
B | GLY361 |
B | SER362 |
B | ARG364 |
B | ILE365 |
B | MG501 |
B | PO4502 |
B | HOH608 |
B | HOH611 |
B | HOH616 |
B | HOH631 |
B | HOH632 |
B | HOH639 |
B | HOH645 |
B | HOH652 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG C 501 |
Chain | Residue |
C | GLU199 |
C | ASP221 |
C | PO4502 |
C | ADP503 |
C | HOH604 |
C | HOH637 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue PO4 C 502 |
Chain | Residue |
C | HOH601 |
C | HOH608 |
C | HOH637 |
C | GLY36 |
C | THR37 |
C | LYS95 |
C | PRO171 |
C | GLU199 |
C | THR226 |
C | MG501 |
C | ADP503 |
site_id | AC9 |
Number of Residues | 24 |
Details | binding site for residue ADP C 503 |
Chain | Residue |
C | GLY36 |
C | THR37 |
C | THR38 |
C | TYR39 |
C | GLY223 |
C | GLY224 |
C | GLY252 |
C | GLU290 |
C | LYS293 |
C | ARG294 |
C | SER297 |
C | GLY360 |
C | GLY361 |
C | SER362 |
C | ARG364 |
C | ASP388 |
C | MG501 |
C | PO4502 |
C | HOH601 |
C | HOH604 |
C | HOH606 |
C | HOH615 |
C | HOH618 |
C | HOH662 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG D 501 |
Chain | Residue |
D | PO4502 |
D | ADP503 |
D | HOH604 |
D | HOH630 |
D | HOH640 |
D | HOH735 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue PO4 D 502 |
Chain | Residue |
D | GLY36 |
D | THR37 |
D | LYS95 |
D | GLU199 |
D | THR226 |
D | MG501 |
D | ADP503 |
D | HOH604 |
D | HOH629 |
D | HOH630 |
D | HOH640 |
site_id | AD3 |
Number of Residues | 27 |
Details | binding site for residue ADP D 503 |
Chain | Residue |
D | GLY36 |
D | THR37 |
D | THR38 |
D | TYR39 |
D | GLY223 |
D | GLY224 |
D | GLY252 |
D | GLU290 |
D | LYS293 |
D | ARG294 |
D | SER297 |
D | GLY360 |
D | GLY361 |
D | SER362 |
D | ARG364 |
D | MG501 |
D | PO4502 |
D | HOH617 |
D | HOH629 |
D | HOH630 |
D | HOH632 |
D | HOH633 |
D | HOH640 |
D | HOH654 |
D | HOH656 |
D | HOH672 |
D | HOH687 |
Functional Information from PROSITE/UniProt
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
Chain | Residue | Details |
A | ILE33-SER40 | |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdvSIL |
Chain | Residue | Details |
A | VAL219-LEU232 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
Chain | Residue | Details |
A | ILE356-GLN370 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LEU53 | |
B | GLY378 | |
C | LEU53 | |
C | SER112 | |
C | VAL241 | |
C | GLU307 | |
C | GLY378 | |
D | LEU53 | |
D | SER112 | |
D | VAL241 | |
D | GLU307 | |
A | SER112 | |
D | GLY378 | |
A | VAL241 | |
A | GLU307 | |
A | GLY378 | |
B | LEU53 | |
B | SER112 | |
B | VAL241 | |
B | GLU307 | |