› 4a2j

X-ray diffraction
2Å resolution

PR X-Ray structures in agonist conformations reveal two different mechanisms for partial agonism in 11beta-substituted steroids

Released:
DOI: 10.2210/pdb4a2j/pdb
PDB entry 4a2j coloured by chain, front view.
PDB entry 4a2j coloured by chain, side view.
PDB entry 4a2j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray structures of progesterone receptor ligand binding domain in its agonist state reveal differing mechanisms for mixed profiles of 11β-substituted steroids.
Lusher SJ, Raaijmakers HC, Vu-Pham D, Kazemier B, Bosch R, McGuire R, Azevedo R, Hamersma H, Dechering K, Oubrie A, van Duin M, de Vlieg J
J Biol Chem 287 20333-43 (2012)
PMID: 22535964

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139037 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Progesterone receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 29.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06401 (Residues: 678-933; Coverage: 27%)
Gene names: NR3C3, PGR
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

2 bound ligands:
Ligand AS0 2 x AS0
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 58.614Å b: 64.696Å c: 69.991Å
α: 90° β: 95.71° γ: 90°
R-values:
R R work R free
0.206 0.204 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Stabilization of protein-protein interactions in drug discovery.
Andrei et al. (2017)
3 more

6 mentions without citation

Structural protein-ligand interaction fingerprints (SPLIF) for structure-based virtual screening: method and benchmark study.
Da et al. (2014)
5 more