1DKG
CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000774 | molecular_function | adenyl-nucleotide exchange factor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006457 | biological_process | protein folding |
| A | 0009408 | biological_process | response to heat |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043335 | biological_process | protein unfolding |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0065003 | biological_process | protein-containing complex assembly |
| B | 0000774 | molecular_function | adenyl-nucleotide exchange factor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006457 | biological_process | protein folding |
| B | 0009408 | biological_process | response to heat |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043335 | biological_process | protein unfolding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0065003 | biological_process | protein-containing complex assembly |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
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 |
| D | ILE7-SER14 |
| site_id | PS00329 |
| Number of Residues | 14 |
| Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSII |
| Chain | Residue | Details |
| D | VAL192-ILE205 |
| site_id | PS01036 |
| Number of Residues | 15 |
| Details | HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK |
| Chain | Residue | Details |
| D | VAL337-LYS351 |
| site_id | PS01071 |
| Number of Residues | 44 |
| Details | GRPE grpE protein signature. LDPnvHqAIamvesddvapgnvlgimqk..GYtln.Grt.IRaAmVtV |
| Chain | Residue | Details |
| A | LEU149-VAL192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interaction with DnaK"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"1835085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8206983","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| 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 |
| D | LYS70 |
