› 1e50

X-ray diffraction
2.6Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-169534 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Runt-related transcription factor 1 Chains: A, C, E, G, Q, R
Molecule details ›
Chains: A, C, E, G, Q, R
Length: 134 amino acids
Theoretical weight: 14.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q01196 (Residues: 50-183; Coverage: 30%)
Gene names: AML1, CBFA2, RUNX1
Sequence domains: Runt domain
Structure domains: Immunoglobulin-like
Core-binding factor subunit beta Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 134 amino acids
Theoretical weight: 15.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13951 (Residues: 2-135; Coverage: 74%)
Gene name: CBFB
Sequence domains: Core binding factor beta subunit
Structure domains: Core binding factor, beta subunit

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 103.26Å b: 79.38Å c: 130.1Å
α: 90° β: 101.39° γ: 90°
R-values:
R R work R free
0.268 0.268 0.287
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

21 review citations

Oncogenic potential of the RUNX gene family: 'overview'.
Ito Y. (2004)
20 more

12 mentions without citation

The three-part model for coding causes and mechanisms of healthcare-related adverse events.
Southern et al. (2022)
11 more