PDBe 2v1d

X-ray diffraction
3.1Å resolution

Structural basis of LSD1-CoREST selectivity in histone H3 recognition

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of LSD1-CoREST selectivity in histone H3 recognition.
J. Biol. Chem. 282 20070-4 (2007)
PMID: 17537733

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Lysine-specific histone demethylase 1A Chain: A
Molecule details ›
Chain: A
Length: 730 amino acids
Theoretical weight: 81.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60341 (Residues: 123-852; Coverage: 86%)
Gene names: AOF2, KDM1, KDM1A, KIAA0601, LSD1
Sequence domains:
Structure domains:
REST corepressor 1 Chain: B
Molecule details ›
Chain: B
Length: 178 amino acids
Theoretical weight: 20.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UKL0 (Residues: 308-485; Coverage: 37%)
Gene names: KIAA0071, RCOR, RCOR1
Sequence domains: Myb-like DNA-binding domain
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
Histone H3.1t Chain: C
Molecule details ›
Chain: C
Length: 21 amino acids
Theoretical weight: 2.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q16695 (Residues: 2-22; Coverage: 15%)
Gene names: H3FT, HIST3H3

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 120.057Å b: 180.496Å c: 233.387Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.223 0.239
Expression systems:
  • Escherichia coli
  • Not provided