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Crystal structures of kinesin mutants reveal a signalling pathway for activation of the motor ATPase

Analyse Crystal structures of kinesin mutants reveal a signalling pathway for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1F9T
Type
protein
Length
304 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein KAR3
UniProt
P17119
Ligands
ADP, MG
Pockets
4 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like protein KAR3protein30436% helix, 31% strandP17119

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1930.500.8327empty
21190.480.8025MG, ADP
3660.300.7415empty
4560.290.7515empty

Compared structures

  • 1F9T · Crystal structures of kinesin mutants reveal a signalling pathway for activation of the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P17119 · AlphaFold monomer V2.0 prediction for kinesin-like protein KAR3 (P17119) · a predicted model of the same protein · chain A against A, TM-score 0.95

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