› 4uda

X-ray diffraction
2.03Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
  • not assigned
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-140042 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mineralocorticoid receptor Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 29.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P08235 (Residues: 735-984; Coverage: 25%)
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: 15 amino acids
Theoretical weight: 1.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q15788 (Residues: 1427-1441; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand DEX 1 x DEX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 73Å b: 81.4Å c: 45.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.24
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Mechanisms of Mitochondrial Redox Signaling in Psychosocial Stress-Responsive Systems: New Insights into an Old Story.
Meyer et al. (2018)
4 more

2 mentions without citation

Getting Docking into Shape Using Negative Image-Based Rescoring.
Kurkinen et al. (2019)
1 more