Dissimilatory sulfite reductase in complex with the endproduct sulfide

Structure

x-ray diffraction · 2 distinct chains · 35% 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
• H2S · Hydrosulfuric acid · ion · chains A

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

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• D–E · 6485 Ų buried · 92 hydrogen bonds · protein-protein
• A–B · 6465 Ų buried · 107 hydrogen bonds · protein-protein
• A–E · 2047 Ų buried · 24 hydrogen bonds · protein-protein
• B–D · 2008 Ų buried · 23 hydrogen bonds · protein-protein
• B–E · 1094 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

• 3MMB · Dissimilatory sulfite reductase in complex with the endproduct sulfide · 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 3MMB · PDBe 3MMB · UniProt Q59109 · UniProt Q59110