PDBe 1pzl

X-ray diffraction
2.1Å resolution

Crystal structure of HNF4a LBD in complex with the ligand and the coactivator SRC-1 peptide

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for HNF-4alpha activation by ligand and coactivator binding.
J. Biol. Chem. 279 23311-6 (2004)
PMID: 14982928

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nuclear receptor coactivator 1 Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.62 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15788 (Residues: 687-700; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1
Hepatocyte nuclear factor 4-alpha Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 26.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P41235 (Residues: 142-378; Coverage: 50%)
Gene names: HNF4, HNF4A, NR2A1, TCF14
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P41212
Unit cell:
a: 81.491Å b: 81.491Å c: 104.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.226 0.267
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)