Research workbench
Cryo-EM structure of BRR2 in complex with JAB1/MPN and C9ORF78
Analyse Cryo-EM structure of BRR2 in complex with JAB1/MPN and C9ORF78 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OS2
- Type
- protein
- Length
- 2,046 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- U5 small nuclear ribonucleoprotein 200 kda helicase; Telomere length and silencing…
- EC
- 3.6.4.13
- UniProt
- O75643, Q9NZ63, Q6P2Q9
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 3 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | U5 small nuclear ribonucleoprotein 200 kda helicase (EC 3.6.4.13) | protein | 1726 | 45% helix, 17% strand | O75643 |
| C | Telomere length and silencing protein 1 homolog | protein | 54 | 57% helix, 6% strand | Q9NZ63 |
| J | Pre-mRNA-processing-splicing factor 8 | protein | 266 | 22% helix, 26% strand | Q6P2Q9 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 871 | 0.85 | 0.87 | 86 | empty |
| 2 | 1158 | 0.83 | 0.84 | 91 | empty |
| 3 | 907 | 0.79 | 0.82 | 80 | empty |
| 4 | 375 | 0.78 | 0.88 | 40 | empty |
| 5 | 126 | 0.76 | 0.95 | 28 | empty |
Interfaces
3 interfaces between chains.
- B–J · 2850 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 2358 Ų buried · 30 hydrogen bonds · protein-protein
- C–J · 62 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7OS2 · Cryo-EM structure of Brr2 in complex with Jab1/MPN and C9ORF78 · the same entry in another collection · chain B against B, TM-score 1.00
- Q9NZ63 · AlphaFold monomer V2.0 prediction for telomere length and silencing protein 1 homolog… · a predicted model of the same protein · chain C against A, TM-score 0.53
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 Q9NZ63
- Every structure of UniProt Q6P2Q9
- Elsewhere: RCSB PDB 7OS2 · PDBe 7OS2 · UniProt O75643 · UniProt Q9NZ63 · UniProt Q6P2Q9
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