› 4rwv

X-ray diffraction
1.86Å resolution

Crystal structure of PIP3 bound human nuclear receptor LRH-1 (Liver Receptor Homolog 1, NR5A2) in complex with a co-regulator DAX-1 (NR0B1) peptide at 1.86 A resolution

Released:
DOI: 10.2210/pdb4rwv/pdb
PDB entry 4rwv coloured by chain, front view.
PDB entry 4rwv coloured by chain, side view.
PDB entry 4rwv coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Joint Center for Structural Genomics (JCSG), Partnership for Stem Cell Biology, Partnership for Stem Cell Biology (STEMCELL)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126308 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nuclear receptor subfamily 5 group A member 2 Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 28.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O00482 (Residues: 294-541; Coverage: 46%)
Gene names: B1F, CPF, FTF, NR5A2
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor subfamily 0 group B member 1 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.65 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P51843 (Residues: 140-154; Coverage: 3%)
Gene names: AHC, DAX1, NR0B1

Ligands and Environments

3 bound ligands:
Ligand PIZ 1 x PIZ
Ligand EDO 5 x EDO
Ligand TRS 1 x TRS
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 71.616Å b: 50.187Å c: 93.608Å
α: 90° β: 109.22° γ: 90°
R-values:
R R work R free
0.173 0.171 0.21
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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