4hlt

X-ray diffraction
1.7Å resolution

Crystal structure of ferric E32V Pirin

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pirin Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 31.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O00625 (Residues: 3-290; Coverage: 99%)
Gene name: PIR
Sequence domains:
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 42.414Å b: 66.635Å c: 107.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.234
Expression system: Escherichia coli BL21