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Cryo-EM MAP of protofilament of microtubule doublet

Analyse Cryo-EM MAP of protofilament of microtubule doublet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UCY
Type
protein
Length
870 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin alpha chain; Tubulin beta chain
UniProt
P41351, P41352
Ligands
GTP, GDP, MG
Pockets
16 · best druggability 0.82

Structure

electron microscopy · 2 distinct chains · 46% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin alpha chainprotein44145% helix, 15% strandP41351
BTubulin beta chainprotein42947% helix, 14% strandP41352

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, B

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11860.820.9743empty
21980.780.9345empty
31010.780.9729empty
4740.750.9824empty
5680.700.9523empty

Interfaces

1 interface between chains.

  • A–B · 1870 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 covalent (covalent ligand).

Compared structures

  • 5UCY · Cryo-EM map of protofilament of microtubule doublet · the same entry in another collection · chain B against B, TM-score 1.00
  • P41352 · AlphaFold monomer V2.0 prediction for tubulin beta chain (P41352) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • P41351 · AlphaFold monomer V2.0 prediction for tubulin alpha chain (P41351) · a predicted model of the same protein · chain A against A, TM-score 0.96

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