6c48

X-ray diffraction
2.32Å resolution

Crystal structure of B-Myb-LIN9-LIN52 complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural mechanism of Myb-MuvB assembly.
Proc. Natl. Acad. Sci. U.S.A. (2018)
PMID: 30224471

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein lin-9 homolog Chains: A, D
Molecule details ›
Chains: A, D
Length: 119 amino acids
Theoretical weight: 14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5TKA1 (Residues: 333-450; Coverage: 22%)
Gene names: BARA, LIN9, TGS
Myb-related protein B Chains: C, F
Molecule details ›
Chains: C, F
Length: 32 amino acids
Theoretical weight: 3.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10244 (Residues: 657-688; Coverage: 5%)
Gene names: BMYB, MYBL2
Protein lin-52 homolog Chains: B, E
Molecule details ›
Chains: B, E
Length: 68 amino acids
Theoretical weight: 7.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q52LA3 (Residues: 52-116; Coverage: 56%)
Gene names: C14orf46, LIN52

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 60.76Å b: 30.77Å c: 105.35Å
α: 90° β: 99.89° γ: 90°
R-values:
R R work R free
0.219 0.217 0.264
Expression system: Escherichia coli