Dissimilatory sulfite reductase carbon monoxide complex

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).

Ligands and binding sites

• SF4 · Iron/sulfur cluster · ligand · 8 copies · chains A, B, D, E
• SRM · Siroheme · ligand · 4 copies · chains A, B, D, E
• CMO · Carbon monoxide · ion · chains A

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

Pockets

16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• D–E · 6406 Ų buried · 98 hydrogen bonds · protein-protein
• A–B · 6394 Ų buried · 110 hydrogen bonds · protein-protein
• A–E · 2039 Ų buried · 24 hydrogen bonds · protein-protein
• B–D · 2010 Ų buried · 21 hydrogen bonds · protein-protein
• B–E · 1103 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

• 3MM7 · Dissimilatory sulfite reductase carbon monoxide complex · the same entry in another collection · chain E against E, TM-score 1.00
• Q59109 · AlphaFold monomer V2.0 prediction for sulfite reductase, dissimilatory-type subunit alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97
• Q59110 · AlphaFold monomer V2.0 prediction for sulfite reductase, dissimilatory-type subunit beta… · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q59109
• Every structure of UniProt Q59110
• Elsewhere: RCSB PDB 3MM7 · PDBe 3MM7 · UniProt Q59109 · UniProt Q59110