PDBe 3tf8

X-ray diffraction
2.13Å resolution

Crystal structure of an H-NOX protein from Nostoc sp. PCC 7120

Released:
Source organism: Nostoc sp. PCC 7120
Primary publication:
Tunnels modulate ligand flux in a heme nitric oxide/oxygen binding (H-NOX) domain.
Proc. Natl. Acad. Sci. U.S.A. 108 E881-9 (2011)
PMID: 21997213

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alr2278 protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 21.21 KDa
Source organism: Nostoc sp. PCC 7120
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8YUQ7 (Residues: 1-189; Coverage: 100%)
Gene name: alr2278
Sequence domains: Haem-NO-binding
Structure domains: H-NOX domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P213
Unit cell:
a: 123.696Å b: 123.696Å c: 123.696Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.2
Expression system: Escherichia coli