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Tubulin alpha-beta dimer, electron diffraction

Analyse Tubulin alpha-beta dimer, electron diffraction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TUB
Type
protein
Length
867 residues
Chains
2
Method
electron crystallography
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin
UniProt
P02550, P02554
Ligands
GTP, GDP, TXL
Pockets
17 · best druggability 0.83

Structure

electron crystallography · 2 distinct chains · 38% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulinprotein44037% helix, 10% strandP02550
BTubulinprotein42739% helix, 10% strandP02554

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · chains A, B
  • GDP · Guanosine-5'-diphosphate · ligand · chains B
  • TXL · Taxotere · ligand · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12680.830.9551GTP
21570.790.9536empty
31930.660.8534empty
43920.650.7950TXL
51110.640.8830empty

Interfaces

1 interface between chains.

  • A–B · 1710 Ų buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

  • 1TUB · Tubulin alpha-beta dimer, electron diffraction · the same entry in another collection · chain A against A, TM-score 1.00
  • P02550 · AlphaFold monomer V2.0 prediction for tubulin alpha-1A chain (P02550) · a predicted model of the same protein · chain A against A, TM-score 0.91

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