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Crystal structure of rev-erb beta
Analyse Crystal structure of rev-erb beta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V0V
- Type
- protein
- Length
- 720 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Orphan nuclear receptor NR1D2
- UniProt
- Q14995
- Pockets
- 10 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Orphan nuclear receptor NR1D2 | protein | 181 | 63% helix, 3% strand | Q14995 |
| C, D | Orphan nuclear receptor NR1D2 | protein | 179 | 60% helix, 2% strand | Q14995 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.55 | 0.74 | 35 | empty |
| 2 | 95 | 0.52 | 0.84 | 28 | empty |
| 3 | 227 | 0.50 | 0.75 | 39 | empty |
| 4 | 56 | 0.40 | 0.81 | 12 | empty |
| 5 | 118 | 0.40 | 0.75 | 22 | empty |
Interfaces
4 interfaces between chains.
- B–C · 474 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 286 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 239 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 185 Ų buried · 1 hydrogen bond · 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 Q14995
- Elsewhere: RCSB PDB 2V0V · PDBe 2V0V · UniProt Q14995
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