› 2b2v

X-ray diffraction
2.65Å resolution

Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4

Released:
DOI: 10.2210/pdb2b2v/pdb
PDB entry 2b2v coloured by chain, front view.
PDB entry 2b2v coloured by chain, side view.
PDB entry 2b2v 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 22.15 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: 13.69 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: 16 amino acids
Theoretical weight: 1.74 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-16; Coverage: 11%)
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
1 modified residue:
Ligand MLZ 1 x MLZ

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 112.255Å b: 54.177Å c: 99.96Å
α: 90° β: 111.97° γ: 90°
R-values:
R R work R free
0.216 0.213 0.266
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

119 review citations

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

2 mentions without citation

Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.
Cieplak AS. (2017)
1 more