› 1cnf

X-ray diffraction
2.7Å resolution

STRUCTURAL STUDIES ON CORN NITRATE REDUCTASE: REFINED STRUCTURE OF THE CYTOCHROME B REDUCTASE FRAGMENT AT 2.5 ANGSTROMS, ITS ADP COMPLEX AND AN ACTIVE SITE MUTANT AND MODELING OF THE CYTOCHROME B DOMAIN

Released:
DOI: 10.2210/pdb1cnf/pdb
PDB entry 1cnf coloured by chain, front view.
PDB entry 1cnf coloured by chain, side view.
PDB entry 1cnf coloured by chain, top view.
Source organism: Zea mays
Primary publication:
Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain.
Lu G, Lindqvist Y, Schneider G, Dwivedi U, Campbell W
J Mol Biol 248 931-48 (1995)
PMID: 7760334

Function and Biology Details

Reaction catalysed: 
Nitrite + NAD(+) + H(2)O = nitrate + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitrate reductase [NADH] 1 Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 30.59 KDa
Source organism: Zea mays
Expression system: Not provided
UniProt:
  • Canonical: P17571 (Residues: 352-621; Coverage: 44%)
Gene name: NNR1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 145.2Å b: 145.2Å c: 47.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 0.272
Expression system: Not provided

Quick links

Citations

9 review citations

The many roles of cytochrome b5.
Schenkman et al. (2003)
8 more

5 mentions without citation

The mononuclear molybdenum enzymes.
Hille et al. (2014)
4 more