› 1g2z

X-ray diffraction
1.15Å resolution

DIMERIZATION DOMAIN OF HNF-1ALPHA WITH A LEU 13 SELENOMETHIONINE SUBSTITUTION

Released:
DOI: 10.2210/pdb1g2z/pdb
PDB entry 1g2z coloured by chain, front view.
PDB entry 1g2z coloured by chain, side view.
PDB entry 1g2z coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
High-resolution structure of the HNF-1alpha dimerization domain.
Rose RB, Endrizzi JA, Cronk JD, Holton J, Alber T
Biochemistry 39 15062-70 (2000)
PMID: 11106484

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte nuclear factor 1-alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 32 amino acids
Theoretical weight: 3.45 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P22361 (Residues: 1-32; Coverage: 5%)
Gene names: Hnf-1, Hnf-1a, Hnf1a, Tcf1

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21212
Unit cell:
a: 37.1Å b: 41.2Å c: 42.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.243
Expression system: Not provided

Quick links

Citations

4 review citations

Protein-protein interactions in multienzyme megasynthetases.
Weissman et al. (2008)
3 more

1 mention without citation

Simultaneous prediction of protein folding and docking at high resolution.
Das et al. (2009)