7XOR
Cryo-EM structure of occupied ring subunit 3 (OR3) of GroEL from GroEL-UGT1A double occupied ring complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
K | 0000287 | molecular_function | magnesium ion binding |
K | 0005515 | molecular_function | protein binding |
K | 0005524 | molecular_function | ATP binding |
K | 0005737 | cellular_component | cytoplasm |
K | 0005829 | cellular_component | cytosol |
K | 0006457 | biological_process | protein folding |
K | 0009314 | biological_process | response to radiation |
K | 0009408 | biological_process | response to heat |
K | 0016020 | cellular_component | membrane |
K | 0016853 | molecular_function | isomerase activity |
K | 0016887 | molecular_function | ATP hydrolysis activity |
K | 0019068 | biological_process | virion assembly |
K | 0042026 | biological_process | protein refolding |
K | 0042802 | molecular_function | identical protein binding |
K | 0051082 | molecular_function | unfolded protein binding |
K | 0051085 | biological_process | chaperone cofactor-dependent protein refolding |
K | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
K | 1990220 | cellular_component | GroEL-GroES complex |
Functional Information from PROSITE/UniProt
site_id | PS00296 |
Number of Residues | 12 |
Details | CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG |
Chain | Residue | Details |
K | ALA405-GLY416 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PCQ, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL |
Chain | Residue | Details |
K | THR30 | |
K | ASP87 | |
K | GLY415 | |
K | ASN479 | |
K | ASP495 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00600, ECO:0000269|PubMed:25174333, ECO:0000305|PubMed:14517228, ECO:0000305|PubMed:9285585, ECO:0007744|PDB:1AON, ECO:0007744|PDB:1PF9, ECO:0007744|PDB:3WVL |
Chain | Residue | Details |
K | LYS51 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
K | LYS34 | |
K | LYS51 | |
K | LYS277 | |
K | LYS321 | |
K | LYS390 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
K | LYS117 |