› 2zn8

X-ray diffraction
2.7Å resolution

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

Released:
DOI: 10.2210/pdb2zn8/pdb
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PDB entry 2zn8 coloured by chain, front view.
PDB entry 2zn8 coloured by chain, side view.
PDB entry 2zn8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism.
Suzuki H, Kawasaki M, Inuzuka T, Okumura M, Kakiuchi T, Shibata H, Wakatsuki S, Maki M
Structure 16 1562-73 (2008)
PMID: 18940611

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-130902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Programmed cell death protein 6 Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75340 (Residues: 2-191; Coverage: 100%)
Gene names: ALG2, PDCD6
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2221
Unit cell:
a: 72.01Å b: 169.738Å c: 46.343Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.211 0.26
Expression system: Escherichia coli

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Citations

9 review citations

The ESCRT complexes.
Hurley JH. (2010)
8 more

4 mentions without citation

Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition.
Inuzuka et al. (2010)
3 more

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