4ewd

X-ray diffraction
2.15Å resolution

Study on structure and function relationships in human Pirin with Mn ion

Released:
Source organism: Homo sapiens
Primary publication:
Pirin is an iron-dependent redox regulator of NF-κB.
Proc. Natl. Acad. Sci. U.S.A. 110 9722-7 (2013)
PMID: 23716661

Function and Biology Details

Reaction catalysed:
Quercetin + O(2) = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H(+)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pirin Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 32.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00625 (Residues: 1-290; Coverage: 100%)
Gene name: PIR
Sequence domains: Pirin C-terminal cupin domain
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 42.332Å b: 67.074Å c: 107.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.234
Expression system: Escherichia coli