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Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules

Analyse Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RZB
Type
protein
Length
1,001 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin alpha-1B chain; Tubulin beta chain; MKIAA0325 protein
UniProt
Q2XVP4, P02554, Q80U36
Ligands
GTP, GDP, TA1, MG
Pockets
9 · best druggability 0.81

Structure

electron microscopy · 3 distinct chains · 48% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin alpha-1B chainprotein42643% helix, 17% strandQ2XVP4
BTubulin beta chainprotein42647% helix, 19% strandP02554
CMKIAA0325 proteinprotein14967% helix, 0% strandQ80U36

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · chains A, B
  • GDP · Guanosine-5'-diphosphate · ligand · chains B
  • TA1 · Taxol · 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

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11870.810.9640GTP, MG
22060.660.8540empty
32980.660.8140empty
42960.590.7827TA1
51970.590.8135GDP

Interfaces

3 interfaces between chains.

  • A–B · 1983 Ų buried · 25 hydrogen bonds · protein-protein
  • B–C · 577 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 509 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 6RZB · Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to… · the same entry in another collection · chain A against A, TM-score 1.00

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