› 1utg

X-ray diffraction
1.34Å resolution

REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1utg/pdb
PDB entry 1utg coloured by chain, front view.
PDB entry 1utg coloured by chain, side view.
PDB entry 1utg coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution.
Morize I, Surcouf E, Vaney MC, Epelboin Y, Buehner M, Fridlansky F, Milgrom E, Mornon JP
J Mol Biol 194 725-39 (1987)
PMID: 3656405

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uteroglobin Chain: A
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 7.91 KDa
Source organism: Oryctolagus cuniculus
Expression system: Not provided
UniProt:
  • Canonical: P02779 (Residues: 22-91; Coverage: 100%)
Gene names: SCGB1A1, UGB, UGL
Sequence domains: Uteroglobin family
Structure domains: Secretoglobin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 50.86Å b: 52.22Å c: 47.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 not available not available
Expression system: Not provided

Quick links

Citations

10 review citations

Protein-protein interactions: a review of protein dimer structures.
Jones et al. (1995)
9 more

29 mentions without citation

Evolution, energy landscapes and the paradoxes of protein folding.
Wolynes PG. (2015)
28 more