Research workbench
Cryo-EM structure of BRR2 in complex with FBP21
Analyse Cryo-EM structure of BRR2 in complex with FBP21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OS1
- Type
- protein
- Length
- 1,746 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U5 small nuclear ribonucleoprotein 200 kda helicase; Ww domain-binding protein 4
- EC
- 3.6.4.13
- UniProt
- O75643, O75554
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | U5 small nuclear ribonucleoprotein 200 kda helicase (EC 3.6.4.13) | protein | 1720 | 45% helix, 17% strand | O75643 |
| F | Ww domain-binding protein 4 | protein | 26 | 0% helix, 4% strand | O75554 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1112 | 0.82 | 0.83 | 93 | empty |
| 2 | 124 | 0.79 | 0.97 | 29 | empty |
| 3 | 480 | 0.76 | 0.84 | 46 | empty |
| 4 | 773 | 0.76 | 0.80 | 83 | empty |
| 5 | 678 | 0.72 | 0.79 | 57 | empty |
Interfaces
1 interface between chains.
- B–F · 1734 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
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 O75643
- Every structure of UniProt O75554
- Elsewhere: RCSB PDB 7OS1 · PDBe 7OS1 · UniProt O75643 · UniProt O75554
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