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Crystal structure of the human KLHL11-CUL3 complex at 3.1A resolution

Analyse Crystal structure of the human KLHL11-CUL3 complex at 3.1A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4APF
Type
protein
Length
605 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kelch-like protein 11; Cullin 3
UniProt
Q9NVR0, Q13618
Pockets
4 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 73% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKelch-like protein 11protein26463% helix, 4% strandQ9NVR0
BCullin 3protein34181% helix, 0% strandQ13618

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.410.8118empty
21150.370.7427empty
3860.330.7418empty
4540.320.7717empty

Interfaces

1 interface between chains.

  • A–B · 1063 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 4APF · Crystal structure of the human KLHL11-Cul3 complex at 3.1A resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13618 · AlphaFold monomer V2.0 prediction for cullin-3 (Q13618) · a predicted model of the same protein · chain B against A, TM-score 0.99
  • Q9NVR0 · AlphaFold monomer V2.0 prediction for kelch-like protein 11 (Q9NVR0) · a predicted model of the same protein · chain A against A, TM-score 0.93

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