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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
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 | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
B | 0051087 | molecular_function | protein-folding chaperone binding |
B | 0065003 | biological_process | protein-containing complex assembly |
D | 0005524 | molecular_function | ATP binding |
D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
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 | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
D | ARG71 | |
D | ASP247 | |
D | GLU360 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
D | MET110 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983 |
Chain | Residue | Details |
D | PHE200 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
D | LYS246 | |
D | LEU305 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1kaz |
Chain | Residue | Details |
D | LYS70 |