6YLF
Rix1-Rea1 pre-60S particle - Rea1, body 3 (rigid body refinement, composite structure of Rea1 ring and tail)
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AP1 | 0000027 | biological_process | ribosomal large subunit assembly |
| AP1 | 0000055 | biological_process | ribosomal large subunit export from nucleus |
| AP1 | 0005515 | molecular_function | protein binding |
| AP1 | 0005524 | molecular_function | ATP binding |
| AP1 | 0005634 | cellular_component | nucleus |
| AP1 | 0005654 | cellular_component | nucleoplasm |
| AP1 | 0005730 | cellular_component | nucleolus |
| AP1 | 0005739 | cellular_component | mitochondrion |
| AP1 | 0006364 | biological_process | rRNA processing |
| AP1 | 0016887 | molecular_function | ATP hydrolysis activity |
| AP1 | 0030687 | cellular_component | preribosome, large subunit precursor |
| AP1 | 0110136 | biological_process | protein-RNA complex remodeling |
| AP1 | 2000200 | biological_process | regulation of ribosomal subunit export from nucleus |
| xP1 | 0000027 | biological_process | ribosomal large subunit assembly |
| xP1 | 0003674 | molecular_function | molecular_function |
| xP1 | 0005515 | molecular_function | protein binding |
| xP1 | 0005634 | cellular_component | nucleus |
| xP1 | 0005730 | cellular_component | nucleolus |
| xP1 | 0042254 | biological_process | ribosome biogenesis |
| xP1 | 0110136 | biological_process | protein-RNA complex remodeling |
Functional Information from PROSITE/UniProt
| site_id | PS00675 |
| Number of Residues | 14 |
| Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLLvGETGTGKttV |
| Chain | Residue | Details |
| AP1 | VAL649-VAL662 |
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. MVTGagDnTARIWDC |
| Chain | Residue | Details |
| xP1 | MET159-CYS173 | |
| xP1 | LEU251-THR265 | |
| xP1 | LEU292-ILE306 | |
| xP1 | ILE417-GLY431 | |
| xP1 | LEU459-VAL473 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| AP1 | GLY315 | |
| AP1 | GLY653 | |
| AP1 | GLY1083 | |
| AP1 | GLY1368 | |
| AP1 | GLY1747 | |
| AP1 | GLY2054 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| AP1 | THR1026 | |
| AP1 | THR4388 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| AP1 | SER2971 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| AP1 | SER4353 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| AP1 | SER4555 |
