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Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide

Analyse Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GY5
Type
protein
Length
296 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kelch-like protein 20; Death-associated protein kinase 1
UniProt
Q9Y2M5
Ligands
NA, CL
Pockets
1 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKelch-like protein 20protein2850% helix, 50% strandQ9Y2M5
UDeath-associated protein kinase 1protein110% helix, 0% strand—

Ligands and binding sites

  • NA · Sodium ion · metal · 14 copies · chains A, U
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 9 copies · chains A, U

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13850.740.8538NA

Interfaces

1 interface between chains.

  • A–U · 540 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6GY5 · Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y2M5 · AlphaFold monomer V2.0 prediction for kelch-like protein 20 (Q9Y2M5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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