› 3ctb

X-ray diffraction
2Å resolution

Tethered PXR-LBD/SRC-1p apoprotein

Released:
DOI: 10.2210/pdb3ctb/pdb
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PDB entry 3ctb coloured by chain, front view.
PDB entry 3ctb coloured by chain, side view.
PDB entry 3ctb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Construction and characterization of a fully active PXR/SRC-1 tethered protein with increased stability.
Wang W, Prosise WW, Chen J, Taremi SS, Le HV, Madison V, Cui X, Thomas A, Cheng KC, Lesburg CA
Protein Eng Des Sel 21 425-33 (2008)
PMID: 18456871

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130964 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear receptor coactivator 1; Nuclear receptor subfamily 1 group I member 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 39.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75469 (Residues: 130-434; Coverage: 70%)
  • Canonical: Q15788 (Residues: 678-700; Coverage: 2%)
Gene names: BHLHE74, NCOA1, NR1I2, PXR, SRC1
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 85.24Å b: 89.24Å c: 105.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.244
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Nuclear receptors CAR and PXR: Molecular, functional, and biomedical aspects.
di Masi et al. (2009)
3 more

9 mentions without citation

Linkers in the structural biology of protein-protein interactions.
Reddy Chichili et al. (2013)
8 more

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