Research workbench
An apo tubulin-rb-ttl complex structure used for side-by-side comparison
Analyse An apo tubulin-rb-ttl complex structure used for side-by-side comparison in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JQG
- Type
- protein
- Length
- 2,149 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1B chain; Tubulin beta chain; Stathmin-4; Uncharacterized protein
- UniProt
- Q2XVP4, P02554, P63043, E1BQ43
- Ligands
- GTP, GDP, ACP, MG, CA, CL
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 6 distinct chains · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 437 | 46% helix, 18% strand | Q2XVP4 |
| B | Tubulin beta chain | protein | 423 | 49% helix, 19% strand | P02554 |
| C | Tubulin alpha-1B chain | protein | 440 | 46% helix, 16% strand | Q2XVP4 |
| D | Tubulin beta chain | protein | 420 | 49% helix, 19% strand | P02554 |
| E | Stathmin-4 | protein | 120 | 77% helix, 14% strand | P63043 |
| F | Uncharacterized protein | protein | 309 | 28% helix, 23% strand | E1BQ43 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 3 copies · chains A, B, C, D
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains F
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 3 copies · chains A, B, C
- CL · Chloride ion · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.83 | 0.84 | 110 | GTP, MG |
| 2 | 1151 | 0.82 | 0.83 | 123 | GDP, MG |
| 3 | 194 | 0.81 | 0.95 | 43 | empty |
| 4 | 1114 | 0.80 | 0.82 | 121 | GTP, MG |
| 5 | 827 | 0.72 | 0.77 | 62 | empty |
Interfaces
9 interfaces between chains.
- A–E · 1580 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1418 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1361 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 907 Ų buried · 15 hydrogen bonds · protein-protein
- C–E · 825 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5JQG · An apo tubulin-RB-TTL complex structure used for side-by-side comparison · 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 Q2XVP4
- Every structure of UniProt P02554
- Every structure of UniProt P63043
- Every structure of UniProt E1BQ43
- Elsewhere: RCSB PDB 5JQG · PDBe 5JQG · UniProt Q2XVP4 · UniProt P02554 · UniProt P63043 · UniProt E1BQ43
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