Research workbench
Crystal structure of human gamma-tubulin bound to GDP
Analyse Crystal structure of human gamma-tubulin bound to GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CB2
- Type
- protein
- Length
- 856 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin gamma-1 chain
- EC
- 3.6.5.6
- UniProt
- P23258
- Ligands
- GDP
- Pockets
- 11 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin gamma-1 chain (EC 3.6.5.6) | protein | 432 | 44% helix, 17% strand | P23258 |
| B | Tubulin gamma-1 chain (EC 3.6.5.6) | protein | 424 | 48% helix, 19% strand | P23258 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.74 | 0.84 | 78 | empty |
| 2 | 309 | 0.64 | 0.80 | 42 | GDP |
| 3 | 239 | 0.60 | 0.80 | 34 | GDP |
| 4 | 242 | 0.60 | 0.80 | 34 | empty |
| 5 | 166 | 0.55 | 0.81 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1547 Ų buried · 10 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 P23258
- Elsewhere: RCSB PDB 3CB2 · PDBe 3CB2 · UniProt P23258
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