Effects of amino acid substitution on three-dimensional structure: an X-ray analysis of cytochrome C3 from desulfovibrio vulgaris hildenborough at 2 ångströms resolution

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 11% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 4 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.

Compared structures

• 2CYM · Effects of amino acid substitution on three-dimensional structure: an X-ray analysis of… · the same entry in another collection · chain A against A, TM-score 1.00
• P00131 · AlphaFold monomer V2.0 prediction for cytochrome C3 (P00131) · a predicted model of the same protein · chain A against A, TM-score 0.98
• 1GX7 · Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase · a predicted model of the same protein · chain A against E, TM-score 0.80
• 1GX7 · Best model of the electron transfer complex between cytochrome C3 and [fe]-hydrogenase · a predicted model of the same protein · chain A against E, TM-score 0.80

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 P00131
• Elsewhere: RCSB PDB 2CYM · PDBe 2CYM · UniProt P00131