2zrt

X-ray diffraction
3.3Å resolution

Crystal structure of Zn2+-bound form of des3-23ALG-2

Released:
Source organism: Homo sapiens
Primary publication:
Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2.
Acta Crystallogr Sect F Struct Biol Cryst Commun 64 974-7 (2008)
PMID: 18997320

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-130902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Programmed cell death protein 6 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 168 amino acids
Theoretical weight: 19.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75340 (Residues: 24-191; Coverage: 88%)
Gene names: ALG2, PDCD6
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 52.806Å b: 147.537Å c: 230.735Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.169 0.221
Expression system: Escherichia coli