› 6sqc

X-ray diffraction
2.28Å resolution

Crystal structure of complex between nuclear coactivator binding domain of CBP and [1040-1086]ACTR containing alpha-methylated Leu1055 and Leu1076

Released:
DOI: 10.2210/pdb6sqc/pdb
Model geometry
Fit model/data
PDB entry 6sqc coloured by chain, front view.
PDB entry 6sqc coloured by chain, side view.
PDB entry 6sqc coloured by chain, top view.
Source organisms:
Primary publication:
Conformational editing of intrinsically disordered protein by α-methylation.
Bauer V, Schmidtgall B, Gógl G, Dolenc J, Osz J, Nominé Y, Kostmann C, Cousido-Siah A, Mitschler A, Rochel N, Travé G, Kieffer B, Torbeev V
OpenAccess logo Chem Sci 12 1080-1089 (2020)
PMID: 34163874

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-279599 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
CREB-binding protein; Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 46.29 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-388, 391-396; Coverage: 100%)
  • Canonical: Q92793 (Residues: 2046-2049, 2061-2112; Coverage: 2%)
Gene names: CBP, CREBBP, JW3994, b4034, malE
Sequence domains:
Nuclear receptor coactivator 3 Chain: B
Molecule details ›
Chain: B
Length: 47 amino acids
Theoretical weight: 5.13 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y6Q9 (Residues: 1045-1091; Coverage: 3%)
Gene names: AIB1, BHLHE42, NCOA3, RAC3, TRAM1
Sequence domains: Nuclear receptor coactivator

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand EDO 1 x EDO
Ligand ZN 2 x ZN
1 modified residue:
Ligand 2ML 2 x 2ML

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 103.18Å b: 42.46Å c: 113.79Å
α: 90° β: 101.125° γ: 90°
R-values:
R R work R free
0.23 0.228 0.274
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 citation in other articles

Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.
Santhouse et al. (2022)
2 more

1 mention without citation

Conformational editing of intrinsically disordered protein by α-methylation.
Bauer et al. (2020)