5svh

X-ray diffraction
2.05Å resolution

Crystal structure of the KIX domain of CBP in complex with a MLL/c-Myb chimera

Released:
Source organisms:
Entry authors: Langelaan DN, Smith SP, Allingham JA

Function and Biology Details

Reactions catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero dodecamer
hetero tetramer
PDBe Complex ID:
PDB-CPX-133941 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CREB-binding protein Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 10.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 587-673; Coverage: 4%)
Gene names: CBP, CREBBP
Sequence domains: KIX domain
Structure domains: Coactivator CBP, KIX domain
MLL cleavage product C180; Transcriptional activator Myb Chain: B
Molecule details ›
Chain: B
Length: 58 amino acids
Theoretical weight: 6.38 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: Q03164 (Residues: 2839-2869; Coverage: 1%)
  • Canonical: P01103 (Residues: 291-315; Coverage: 4%)
Gene names: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL, MLL1, MYB, TRX1
Sequence domains: LMSTEN motif

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P6322
Unit cell:
a: 119.82Å b: 119.82Å c: 50.43Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.206 0.242
Expression system: Escherichia coli