Research workbench
3D structure of the human ruvb-like helicase RUVBL1
Analyse 3D structure of the human ruvb-like helicase RUVBL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C9O
- Type
- protein
- Length
- 1,102 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ruvb-like 1
- EC
- 3.6.1.-
- UniProt
- Q9Y265
- Ligands
- ADP
- Pockets
- 15 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ruvb-like 1 (EC 3.6.1.-) | protein | 398 | 39% helix, 27% strand | Q9Y265 |
| B | Ruvb-like 1 (EC 3.6.1.-) | protein | 393 | 39% helix, 28% strand | Q9Y265 |
| C | Ruvb-like 1 (EC 3.6.1.-) | protein | 311 | 46% helix, 20% strand | Q9Y265 |
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
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 899 | 0.85 | 0.87 | 99 | ADP |
| 2 | 291 | 0.71 | 0.84 | 40 | ADP |
| 3 | 253 | 0.68 | 0.84 | 37 | ADP |
| 4 | 143 | 0.59 | 0.84 | 29 | empty |
| 5 | 320 | 0.57 | 0.76 | 50 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1822 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1437 Ų buried · 21 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 Q9Y265
- Elsewhere: RCSB PDB 2C9O · PDBe 2C9O · UniProt Q9Y265
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