Research workbench
Tubulin-B2 complex
Analyse Tubulin-B2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SES
- Type
- protein
- Length
- 2,163 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1B chain; Tubulin beta-2B chain; Stathmin-4; Tubulin-tyrosine ligase
- UniProt
- P81947, Q6B856, P63043, E1BQ43
- Ligands
- GTP, GDP, L95, ACP, MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 6 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 438 | 47% helix, 18% strand | P81947 |
| B | Tubulin beta-2B chain | protein | 425 | 49% helix, 19% strand | Q6B856 |
| C | Tubulin alpha-1B chain | protein | 440 | 47% helix, 17% strand | P81947 |
| D | Tubulin beta-2B chain | protein | 424 | 49% helix, 19% strand | Q6B856 |
| E | Stathmin-4 | protein | 123 | 76% helix, 13% strand | P63043 |
| F | Tubulin-tyrosine ligase | protein | 313 | 32% helix, 26% strand | E1BQ43 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B, C, D
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains B, D
- L95 · [(3~{Z},5~{S},6~{S},7~{S},8~{R},9~{S},11~{Z},13~{S}, 14~{S},15~{S},16~{Z},18~{S})-5,7,9,11,13,15-hexamethyl-19-[(2~{S},3~{R})-3-methyl-6-oxidanylidene-oxan-2-yl]-8,14,18-tris(oxidanyl)nonadeca-3,11,16-trien-6-yl] carbamate · ligand · 2 copies · chains B, D
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains F
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, F
- GOL · Glycerol · additive · chains A, E
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1112 | 0.84 | 0.85 | 133 | GTP, MG |
| 2 | 1162 | 0.83 | 0.84 | 130 | GDP, MG |
| 3 | 1008 | 0.80 | 0.81 | 108 | GTP, MG |
| 4 | 841 | 0.73 | 0.78 | 62 | empty |
| 5 | 73 | 0.71 | 0.96 | 23 | empty |
Interfaces
9 interfaces between chains.
- A–E · 1623 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 1465 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1394 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 996 Ų buried · 16 hydrogen bonds · protein-protein
- A–F · 826 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 6SES · Tubulin-B2 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 P81947
- Every structure of UniProt Q6B856
- Every structure of UniProt P63043
- Every structure of UniProt E1BQ43
- Elsewhere: RCSB PDB 6SES · PDBe 6SES · UniProt P81947 · UniProt Q6B856 · UniProt P63043 · UniProt E1BQ43
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