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Cryo-EM structure of KIFBP:KIF15

Analyse Cryo-EM structure of KIFBP:KIF15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RYP
Type
protein
Length
725 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kinesin-like protein KIF15; Kif-binding protein
UniProt
Q9NS87, Q96EK5
Pockets
15 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 55% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKinesin-like protein KIF15protein33330% helix, 22% strandQ9NS87
BKif-binding proteinprotein39276% helix, 0% strandQ96EK5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18800.860.88108empty
27630.780.8272empty
37280.750.8089empty
45970.740.8153empty
51780.700.8826empty

Interfaces

1 interface between chains.

  • A–B · 856 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7RYP · Cryo-EM structure of KIFBP:KIF15 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96EK5 · AlphaFold monomer V2.0 prediction for kif-binding protein (Q96EK5) · a predicted model of the same protein · chain B against A, TM-score 0.83
  • Q9NS87 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF15 (Q9NS87) · a predicted model of the same protein · chain A against A, TM-score 0.80

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