2QWR
Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the AMPPNP intact form
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ANP A 487 |
| Chain | Residue |
| A | ASP10 |
| A | THR204 |
| A | GLY230 |
| A | GLU268 |
| A | LYS271 |
| A | ARG272 |
| A | SER275 |
| A | GLY338 |
| A | GLY339 |
| A | SER340 |
| A | ARG342 |
| A | GLY12 |
| A | ILE343 |
| A | GOL3148 |
| A | HOH3180 |
| A | HOH3209 |
| A | THR13 |
| A | THR14 |
| A | TYR15 |
| A | GLU175 |
| A | ASP199 |
| A | GLY201 |
| A | GLY202 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 1022 |
| Chain | Residue |
| A | ASP32 |
| A | LYS126 |
| A | ILE130 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3147 |
| Chain | Residue |
| A | THR13 |
| A | LYS71 |
| A | ARG72 |
| A | TYR149 |
| A | PHE150 |
| A | THR226 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 3148 |
| Chain | Residue |
| A | TYR15 |
| A | LYS56 |
| A | GLU231 |
| A | ASP234 |
| A | GLU268 |
| A | ANP487 |
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 | 191 |
| Details | Region: {"description":"Interaction with BAG1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| 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 | 2 |
| 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 | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11142","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 656 |
| Chain | Residue | Details |
| A | ASP10 | |
| A | LYS71 | enhance reactivity |
| A | GLU175 | |
| A | ASP199 |
