› 1m1d

X-ray diffraction
2.2Å resolution

TETRAHYMENA GCN5 WITH BOUND BISUBSTRATE ANALOG INHIBITOR

Released:
DOI: 10.2210/pdb1m1d/pdb
PDB entry 1m1d coloured by chain, front view.
PDB entry 1m1d coloured by chain, side view.
PDB entry 1m1d coloured by chain, top view.
Source organisms:
Primary publication:
Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor.
Poux AN, Cebrat M, Kim CM, Cole PA, Marmorstein R
Proc Natl Acad Sci U S A 99 14065-70 (2002)
PMID: 12391296

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158415 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase GCN5 Chains: A, C
Molecule details ›
Chains: A, C
Length: 163 amino acids
Theoretical weight: 19.46 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q27198 (Residues: 48-209; Coverage: 39%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase
Histone H3 Chains: B, D
Molecule details ›
Chains: B, D
Length: 20 amino acids
Theoretical weight: 3.01 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P61830 (Residues: 2-21; Coverage: 15%)
Gene names: HHT1, HHT2, N2749, SIN2, YBR010W, YBR0201, YNL031C

Ligands and Environments

No bound ligands
1 modified residue:
Ligand LYX 2 x LYX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 67.42Å b: 67.83Å c: 74.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.271 0.213 0.265
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

17 review citations

Structure and functions of the GNAT superfamily of acetyltransferases.
Vetting et al. (2005)
16 more

9 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
8 more