MolNFT v1 · #32546 · protein
Structure of btubab heterodimer from prosthecobacter dejongeii
2BTQ · Tubulin btuba: “Structure of btubab heterodimer from prosthecobacter dejongeii”. X-ray diffraction, 2 ligands (GDP, SO4), 9 pockets (best druggability 0.81). MolNFT v1 #32546 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2BTQ
- Type
- protein
- Length
- 827 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin btuba; Tubulin btubb
- UniProt
- Q8GCC5, Q8GCC1
- Ligands
- GDP, SO4
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin btuba | protein | 436 | 46% helix, 17% strand | Q8GCC5 |
| B | Tubulin btubb | protein | 391 | 44% helix, 20% strand | Q8GCC1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 937 | 0.81 | 0.83 | 87 | SO4 |
| 2 | 247 | 0.63 | 0.82 | 35 | GDP |
| 3 | 143 | 0.49 | 0.78 | 26 | empty |
| 4 | 67 | 0.48 | 0.84 | 19 | empty |
| 5 | 72 | 0.48 | 0.83 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1269 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2BTQ · Structure of BtubAB heterodimer from Prosthecobacter dejongeii · 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 Q8GCC5
- Every structure of UniProt Q8GCC1
- Elsewhere: RCSB PDB 2BTQ · PDBe 2BTQ · UniProt Q8GCC5 · UniProt Q8GCC1
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