Research workbench
Structure of RCL1P - BMS1P complex
Analyse Structure of RCL1P - BMS1P complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CLQ
- Type
- protein
- Length
- 409 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA 3'-terminal phosphate cyclase-like protein; Ribosome biogenesis protein BMS1
- UniProt
- Q08096, Q08965
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA 3'-terminal phosphate cyclase-like protein | protein | 355 | 31% helix, 28% strand | Q08096 |
| B | Ribosome biogenesis protein BMS1 | protein | 54 | 48% helix, 2% strand | Q08965 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.41 | 0.75 | 24 | empty |
| 2 | 110 | 0.36 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2405 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 4CLQ · Structure of Rcl1p - Bms1p complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q08096 · AlphaFold monomer V2.0 prediction for RNA 3'-terminal phosphate cyclase-like protein… · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q08965 · AlphaFold monomer V2.0 prediction for ribosome biogenesis protein BMS1 (Q08965) · a predicted model of the same protein · chain B against A, TM-score 0.67
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q08096
- Every structure of UniProt Q08965
- Elsewhere: RCSB PDB 4CLQ · PDBe 4CLQ · UniProt Q08096 · UniProt Q08965
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