Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 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 401 |
Chain | Residue |
A | LYS138 |
A | ARG150 |
A | ILE151 |
A | HOH514 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ASN204 |
A | ARG205 |
A | HOH567 |
A | HOH660 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | ASP131 |
A | HOH654 |
A | ASN130 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue SO4 A 404 |
Chain | Residue |
A | TYR128 |
A | ASP184 |
A | GLY202 |
A | ASP203 |
A | ASN204 |
A | HOH558 |
A | HOH569 |
A | HOH588 |
A | HOH598 |
A | HOH655 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue SO4 A 405 |
Chain | Residue |
A | GLY14 |
A | THR15 |
A | THR16 |
A | ASN17 |
A | LYS72 |
A | PRO126 |
A | GLY179 |
A | GLY180 |
A | THR182 |
A | HOH505 |
A | HOH512 |
A | HOH546 |
A | HOH561 |
A | HOH590 |
A | HOH609 |
A | HOH617 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 406 |
Chain | Residue |
A | VAL29 |
A | VAL30 |
A | ARG38 |
A | HOH591 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | LYS116 |
A | LYS341 |
A | ARG364 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PGE A 408 |
Chain | Residue |
A | SER70 |
A | ARG73 |
A | LEU74 |
A | ARG205 |
A | HOH538 |
A | HOH594 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | THR15 |
A | LYS72 |
A | ARG73 |
A | TYR128 |
A | PHE129 |
A | HOH501 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL A 410 |
Chain | Residue |
A | TYR162 |
A | GLY163 |
A | ALA167 |
A | GLU316 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 411 |
Chain | Residue |
A | LYS214 |
A | MET237 |
A | PRO291 |
A | LEU292 |
A | ARG295 |
A | HOH599 |
A | HOH639 |
Functional Information from PROSITE/UniProt
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS |
Chain | Residue | Details |
A | ILE11-SER18 | |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdvSLL |
Chain | Residue | Details |
A | VAL175-LEU188 | |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IlLvGGsTRMPaVqK |
Chain | Residue | Details |
A | ILE317-LYS331 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | THR182 | |