PDBe 2a3i

X-ray diffraction
1.95Å resolution

Structural and Biochemical Mechanisms for the Specificity of Hormone Binding and Coactivator Assembly by Mineralocorticoid Receptor

Released:

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):
Mineralocorticoid receptor Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 29.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08235 (Residues: 732-984; Coverage: 26%)
Gene names: MCR, MLR, NR3C2
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor coactivator 1 Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15788 (Residues: 1430-1441; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 44.647Å b: 72.259Å c: 81.226Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.253
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided