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Crystal structure of the candida albicans kinesin-8 motor domain

Analyse Crystal structure of the candida albicans kinesin-8 motor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LFF
Type
protein
Length
663 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein
UniProt
A0A1D8PKA4
Ligands
ADP, MG
Pockets
8 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like proteinprotein33131% helix, 27% strandA0A1D8PKA4
BKinesin-like proteinprotein33230% helix, 27% strandA0A1D8PKA4

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11210.560.8427empty
2880.540.8526empty
31120.410.7624ADP, MG
41230.400.7524MG
5890.360.7518empty

Interfaces

1 interface between chains.

  • A–B · 1031 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 7LFF · Crystal structure of the Candida albicans kinesin-8 motor domain · the same entry in another collection · chain A against A, TM-score 1.00

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