3kb5

X-ray diffraction
1.5Å resolution

PRY-SPRY domain of human TRIM72

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of PRY-SPRY domain of human TRIM72.
Proteins 78 790-5 (2010)
PMID: 19967786

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tripartite motif-containing protein 72 Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 21.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6ZMU5 (Residues: 278-470; Coverage: 41%)
Gene names: MG53, TRIM72
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A, PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 153.747Å b: 35.937Å c: 33.2Å
α: 90° β: 99.87° γ: 90°
R-values:
R R work R free
0.219 0.219 0.237
Expression system: Escherichia coli