› 4aya

X-ray diffraction
2.1Å resolution

Crystal structure of ID2 HLH homodimer at 2.1A resolution

Released:
DOI: 10.2210/pdb4aya/pdb
PDB entry 4aya coloured by chain, front view.
PDB entry 4aya coloured by chain, side view.
PDB entry 4aya coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A divalent ion is crucial in the structure and dominant-negative function of ID proteins, a class of helix-loop-helix transcription regulators.
Wong MV, Jiang S, Palasingam P, Kolatkar PR
PLoS One 7 e48591 (2012)
PMID: 23119064

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-binding protein inhibitor ID-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 97 amino acids
Theoretical weight: 10.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02363 (Residues: 1-82; Coverage: 61%)
Gene names: BHLHB26, ID2
Sequence domains: Helix-loop-helix DNA-binding domain
Structure domains: Helix-loop-helix DNA-binding domain

Ligands and Environments

2 bound ligands:
Ligand K 2 x K
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3221
Unit cell:
a: 51.622Å b: 51.622Å c: 111.474Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.225 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Id proteins: emerging roles in CNS disease and targets for modifying neural stemcell behavior.
Chu et al. (2022)
7 other articles

7 mentions without citation

The Id-protein family in developmental and cancer-associated pathways.
Roschger et al. (2017)
6 more