› 2b2t

X-ray diffraction
2.45Å resolution

Tandem chromodomains of human CHD1 complexed with Histone H3 Tail containing trimethyllysine 4 and phosphothreonine 3

Released:
DOI: 10.2210/pdb2b2t/pdb
PDB entry 2b2t coloured by chain, front view.
PDB entry 2b2t coloured by chain, side view.
PDB entry 2b2t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Double chromodomains cooperate to recognize the methylated histone H3 tail.
Flanagan JF, Mi LZ, Chruszcz M, Cymborowski M, Clines KL, Kim Y, Minor W, Rastinejad F, Khorasanizadeh S
Nature 438 1181-5 (2005)
PMID: 16372014

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127040 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chromodomain-helicase-DNA-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 187 amino acids
Theoretical weight: 22.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14646 (Residues: 268-443; Coverage: 10%)
Gene name: CHD1
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Chromodomain-helicase-DNA-binding protein 1 Chain: C
Molecule details ›
Chain: C
Length: 115 amino acids
Theoretical weight: 13.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14646 (Residues: 268-373; Coverage: 6%)
Gene name: CHD1
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Histone H3.1 Chain: D
Molecule details ›
Chain: D
Length: 20 amino acids
Theoretical weight: 2.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-20; Coverage: 14%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

No bound ligands
3 modified residues:
Ligand MSE 11 x MSE
Ligand TPO 1 x TPO
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID, null
Spacegroup: C2
Unit cell:
a: 111.986Å b: 54.686Å c: 100.989Å
α: 90° β: 112.15° γ: 90°
R-values:
R R work R free
0.218 0.218 0.266
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

118 review citations

The biology of chromatin remodeling complexes.
Clapier et al. (2009)
117 more

2 mentions without citation

The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.
Dreveny et al. (2014)
1 more