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Yeast tubulin polymerized with GTP in vitro

Analyse Yeast tubulin polymerized with GTP in vitro in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W3F
Type
protein
Length
867 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.7
Source
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Molecule
Tubulin alpha-1 chain; Tubulin beta chain
UniProt
P09733, P02557
Ligands
GTP, GDP, MG
Pockets
11 · best druggability 0.82

Structure

electron microscopy · resolution 3.7 · 2 distinct chains · 43% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin alpha-1 chainprotein44044% helix, 16% strandP09733
BTubulin beta chainprotein42741% helix, 11% strandP02557

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · chains A, B
  • GDP · Guanosine-5'-diphosphate · ligand · chains B
  • MG · Magnesium ion · metal · chains A

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16130.820.8781MG, GTP
2740.660.9234empty
33220.640.8038GDP
42550.580.7941empty
5720.550.8818empty

Interfaces

1 interface between chains.

  • A–B · 1775 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 5W3F · Yeast tubulin polymerized with GTP in vitro · the same entry in another collection · chain A against A, TM-score 1.00
  • P09733 · AlphaFold monomer V2.0 prediction for tubulin alpha-1 chain (P09733) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • P02557 · AlphaFold monomer V2.0 prediction for tubulin beta chain (P02557) · a predicted model of the same protein · chain B against A, TM-score 0.96

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