6gy5

X-ray diffraction
1.09Å resolution

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

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-156789 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Kelch-like protein 20 Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 33.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y2M5 (Residues: 303-605; Coverage: 50%)
Gene names: KLEIP, KLHL20, KLHLX
Sequence domains: Kelch motif
Structure domains: Kelch-type beta propeller
Death-associated protein kinase 1 Chain: U
Molecule details ›
Chain: U
Length: 11 amino acids
Theoretical weight: 1.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P53355 (Residues: 1334-1344; Coverage: 1%)
Gene names: DAPK, DAPK1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 40.459Å b: 47.361Å c: 151.933Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.172
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided