1NGC
STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 487 |
| Chain | Residue |
| A | ADP486 |
| A | PO4488 |
| A | HOH577 |
| A | HOH578 |
| A | HOH579 |
| A | HOH626 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 488 |
| Chain | Residue |
| A | GLU175 |
| A | THR204 |
| A | ADP486 |
| A | MG487 |
| A | HOH578 |
| A | HOH626 |
| A | GLY12 |
| A | THR13 |
| A | LYS71 |
| site_id | AC3 |
| 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 | ILE343 |
| A | ASP366 |
| A | MG487 |
| A | PO4488 |
| A | HOH537 |
| A | HOH549 |
| A | HOH551 |
| A | HOH568 |
| A | HOH577 |
| A | HOH579 |
| A | HOH580 |
| A | HOH581 |
| A | HOH626 |
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. IFDLGGGTfsvSIL |
| 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 |
