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Apo CAKIP3[2-482] in complex with a microtubule

Analyse Apo CAKIP3[2-482] in complex with a microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TQZ
Type
protein
Length
1,229 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin alpha-1B chain; Tubulin beta-2B chain; Kinesin-like protein
UniProt
Q2XVP4, A0A287AGU7, A0A1D8PKA4
Ligands
GTP, GDP, TA1, MG
Pockets
19 · best druggability 0.84

Structure

electron microscopy · 3 distinct chains · 42% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin alpha-1B chainprotein44043% helix, 18% strandQ2XVP4
BTubulin beta-2B chainprotein42948% helix, 18% strandA0A287AGU7
KKinesin-like proteinprotein36032% helix, 24% strandA0A1D8PKA4

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.840.9642GTP
211530.790.8181empty
33840.700.8262empty
45010.680.7963empty
52460.610.8135GDP

Interfaces

3 interfaces between chains.

  • A–B · 1982 Ų buried · 26 hydrogen bonds · protein-protein
  • A–K · 1332 Ų buried · 22 hydrogen bonds · protein-protein
  • B–K · 626 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7TQZ · Apo CaKip3[2-482] in complex with a microtubule · the same entry in another collection · chain A against A, TM-score 1.00

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