Research workbench
Tubulin-RB3_SLD-ttl in complex with compound abi-274
Analyse Tubulin-RB3_SLD-ttl in complex with compound abi-274 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PC4
- Type
- protein
- Length
- 2,178 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
- Q2XVP4, A0A287AGU7, Q9H169, E1BQ43
- Ligands
- GTP, GDP, O91, MG, CA
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 6 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 437 | 46% helix, 18% strand | Q2XVP4 |
| B | Tubulin beta-2B chain | protein | 427 | 47% helix, 19% strand | A0A287AGU7 |
| C | Tubulin alpha-1B chain | protein | 440 | 47% helix, 17% strand | Q2XVP4 |
| D | Tubulin beta-2B chain | protein | 421 | 49% helix, 19% strand | A0A287AGU7 |
| E | Stathmin-4 | protein | 121 | 76% helix, 13% strand | Q9H169 |
| F | Tubulin tyrosine ligase | protein | 332 | 31% helix, 21% 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
- O91 · [2-(4-methylphenyl)-1H-imidazol-4-yl](3,4,5-trimethoxyphenyl)methanone · ligand · 2 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 3 copies · chains A, B, C, D
- CA · Calcium ion · metal · 2 copies · chains A, C
- 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, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.87 | 0.89 | 138 | GTP, MG, O91 |
| 2 | 672 | 0.82 | 0.86 | 90 | GDP, MG |
| 3 | 673 | 0.81 | 0.85 | 83 | O91 |
| 4 | 187 | 0.80 | 0.95 | 37 | GTP, MG |
| 5 | 77 | 0.72 | 0.96 | 22 | empty |
Interfaces
9 interfaces between chains.
- A–E · 1671 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1520 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1368 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 916 Ų buried · 14 hydrogen bonds · protein-protein
- C–E · 850 Ų buried · 9 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 Q2XVP4
- Every structure of UniProt A0A287AGU7
- Every structure of UniProt Q9H169
- Every structure of UniProt E1BQ43
- Elsewhere: RCSB PDB 6PC4 · PDBe 6PC4 · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt Q9H169 · UniProt E1BQ43
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