The 0.91 a resolution structure of the L16G mutant of cytochrome C prime from alcaligenes xylosoxidans, complexed with nitric oxide

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

Ligands and binding sites

• HEC · Heme C · ligand · chains A
• SO4 · Sulfate ion · ion · 4 copies · chains A
• NO2 · Nitrite ion · ion · 2 copies · chains A
• NO · Nitric oxide · ion · chains A
• NO3 · Nitrate ion · ion · chains A
• EDO · 1,2-ethanediol · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 2 cofactor, 1 modified (heme c attachment, cyclization).

Compared structures

• 5NC0 · The 0.91 A resolution structure of the L16G mutant of cytochrome c prime from Alcaligenes… · the same entry in another collection · chain A against A, TM-score 1.00
• P00138 · AlphaFold monomer V2.0 prediction for cytochrome C' (P00138) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P00138
• Elsewhere: RCSB PDB 5NC0 · PDBe 5NC0 · UniProt P00138