1p32

X-ray diffraction
2.25Å resolution

CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein.
Proc. Natl. Acad. Sci. U.S.A. 96 3572-7 (1999)
PMID: 10097078

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement component 1 Q subcomponent-binding protein, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 209 amino acids
Theoretical weight: 23.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07021 (Residues: 74-282; Coverage: 74%)
Gene names: C1QBP, GC1QBP, HABP1, SF2P32
Sequence domains: Mitochondrial glycoprotein
Structure domains: Mitochondrial glycoprotein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 58.625Å b: 56.481Å c: 93.831Å
α: 90° β: 95.99° γ: 90°
R-values:
R R work R free
0.173 0.173 0.234
Expression system: Escherichia coli