Research workbench
Tubulin:iE5 alphaRep complex
Analyse Tubulin:iE5 alphaRep complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GWC
- Type
- protein
- Length
- 1,065 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Ovis aries; synthetic construct
- Molecule
- Alpha-tubulin; Tubulin beta chain; iE5 ALPHAREP
- UniProt
- D0VWY9
- Ligands
- GTP, MG
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.6 · 3 distinct chains · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tubulin | protein | 431 | 45% helix, 18% strand | — |
| B | Tubulin beta chain | protein | 417 | 49% helix, 19% strand | D0VWY9 |
| C | iE5 ALPHAREP | protein | 217 | 81% helix, 0% strand | — |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.80 | 0.81 | 113 | GTP, MG, PGE |
| 2 | 258 | 0.62 | 0.81 | 37 | empty |
| 3 | 151 | 0.61 | 0.85 | 33 | empty |
| 4 | 176 | 0.61 | 0.83 | 34 | GTP, MG |
| 5 | 309 | 0.57 | 0.76 | 33 | empty |
Interfaces
2 interfaces between chains.
- A–C · 1308 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1271 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6GWC · TUBULIN:IE5 alpharep complex · the same entry in another collection · chain A against A, TM-score 1.00
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 D0VWY9
- Elsewhere: RCSB PDB 6GWC · PDBe 6GWC · UniProt D0VWY9
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