Research workbench
RUVBL1-RUVBL2 heterohexameric ring after binding of RNA helicase DHX34
Analyse RUVBL1-RUVBL2 heterohexameric ring after binding of RNA helicase DHX34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AHO
- Type
- protein
- Length
- 1,748 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ruvb-like 1; Ruvb-like 2
- EC
- 3.6.4.12
- UniProt
- Q9Y265, Q9Y230
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 6 distinct chains · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ruvb-like 1 (EC 3.6.4.12) | protein | 305 | 41% helix, 16% strand | Q9Y265 |
| B | Ruvb-like 1 (EC 3.6.4.12) | protein | 299 | 44% helix, 13% strand | Q9Y265 |
| C | Ruvb-like 1 (EC 3.6.4.12) | protein | 306 | 39% helix, 15% strand | Q9Y265 |
| D | Ruvb-like 2 (EC 3.6.4.12) | protein | 283 | 37% helix, 10% strand | Q9Y230 |
| E | Ruvb-like 2 (EC 3.6.4.12) | protein | 273 | 38% helix, 13% strand | Q9Y230 |
| F | Ruvb-like 2 (EC 3.6.4.12) | protein | 282 | 39% helix, 16% strand | Q9Y230 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 846 | 0.84 | 0.86 | 89 | ADP |
| 2 | 569 | 0.81 | 0.87 | 57 | ADP |
| 3 | 906 | 0.75 | 0.78 | 76 | empty |
| 4 | 962 | 0.74 | 0.77 | 82 | empty |
| 5 | 283 | 0.73 | 0.86 | 31 | empty |
Interfaces
7 interfaces between chains.
- A–F · 2032 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1964 Ų buried · 14 hydrogen bonds · protein-protein
- C–F · 1952 Ų buried · 16 hydrogen bonds · protein-protein
- C–E · 1894 Ų buried · 20 hydrogen bonds · protein-protein
- B–E · 1794 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 Q9Y265
- Every structure of UniProt Q9Y230
- Elsewhere: RCSB PDB 7AHO · PDBe 7AHO · UniProt Q9Y265 · UniProt Q9Y230
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