2QWL
Crystal structure of bovine hsc70 (1-394aa)in the ADP state
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 587 |
Chain | Residue |
A | ADP486 |
A | NA589 |
A | HOH596 |
A | HOH654 |
A | HOH683 |
A | HOH686 |
A | HOH722 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 687 |
Chain | Residue |
B | HOH691 |
B | HOH738 |
B | HOH785 |
B | HOH828 |
B | HOH904 |
B | ADP486 |
B | NA689 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 589 |
Chain | Residue |
A | ASP10 |
A | TYR15 |
A | ADP486 |
A | MG587 |
A | HOH690 |
A | HOH722 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 590 |
Chain | Residue |
A | ASP199 |
A | THR204 |
A | ASP206 |
A | HOH596 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 689 |
Chain | Residue |
B | ASP10 |
B | TYR15 |
B | ADP486 |
B | MG687 |
B | HOH787 |
B | HOH904 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 690 |
Chain | Residue |
B | ASP199 |
B | THR204 |
B | ASP206 |
B | HOH691 |
site_id | AC7 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ADP A 486 |
Chain | Residue |
A | THR13 |
A | THR14 |
A | TYR15 |
A | GLY201 |
A | GLY202 |
A | GLY230 |
A | GLU268 |
A | LYS271 |
A | ARG272 |
A | SER275 |
A | GLY338 |
A | GLY339 |
A | SER340 |
A | ARG342 |
A | ASP366 |
A | MG587 |
A | NA589 |
A | HOH596 |
A | HOH628 |
A | HOH630 |
A | HOH653 |
A | HOH654 |
A | HOH683 |
A | HOH690 |
A | HOH717 |
A | HOH722 |
A | HOH747 |
site_id | AC8 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE ADP B 486 |
Chain | Residue |
B | THR13 |
B | THR14 |
B | TYR15 |
B | GLY201 |
B | GLY202 |
B | GLY230 |
B | GLU268 |
B | LYS271 |
B | ARG272 |
B | SER275 |
B | GLY338 |
B | GLY339 |
B | SER340 |
B | ARG342 |
B | ILE343 |
B | ASP366 |
B | MG687 |
B | NA689 |
B | HOH691 |
B | HOH715 |
B | HOH735 |
B | HOH738 |
B | HOH752 |
B | HOH785 |
B | HOH787 |
B | HOH851 |
B | HOH889 |
B | HOH904 |
B | HOH1065 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 1 |
Chain | Residue |
B | HOH842 |
A | GLU318 |
A | LYS328 |
A | PHE353 |
A | HOH860 |
B | ARG311 |
B | LEU349 |
B | ASP352 |
B | PHE353 |
B | HOH736 |
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 | ILE9-SER16 |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. IFDLGGGTfdvSIL |
Chain | Residue | Details |
A | ILE197-LEU210 |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqK |
Chain | Residue | Details |
A | ILE334-LYS348 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 382 |
Details | Region: {"description":"Interaction with BAG1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PDB","id":"2QWL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QWQ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P63017","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1kaz |
Chain | Residue | Details |
A | LYS71 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1kaz |
Chain | Residue | Details |
B | LYS71 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 656 |
Chain | Residue | Details |
A | ASP10 | |
A | LYS71 | enhance reactivity |
A | GLU175 | |
A | ASP199 |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 656 |
Chain | Residue | Details |
B | ASP10 | |
B | LYS71 | enhance reactivity |
B | GLU175 | |
B | ASP199 |