Research workbench
Crystal structure of SULFIDE:QUINONE oxidoreductase SER126ALA variant from acidithiobacillus ferrooxidans using 7.0 kev diffraction data
Analyse Crystal structure of SULFIDE:QUINONE oxidoreductase SER126ALA variant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SYI
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfide-quinone reductase, putative
- UniProt
- B7JBP8
- Ligands
- FAD, H2S, SO4
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfide-quinone reductase, putative | protein | 421 | 31% helix, 26% strand | B7JBP8 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- H2S · Hydrosulfuric acid · ion · 5 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- LMT · Dodecyl-beta-D-maltoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1067 | 0.82 | 0.83 | 105 | FAD, H2S |
| 2 | 170 | 0.65 | 0.85 | 29 | LMT |
| 3 | 61 | 0.30 | 0.75 | 15 | empty |
Compared structures
- 3SYI · Crystal structure of sulfide:qui oxidoreductase Ser126Ala variant from Acidithiobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- B7JBP8 · AlphaFold monomer V2.0 prediction for sulfide-quinone reductase (B7JBP8) · a predicted model of the same protein · chain A 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 B7JBP8
- Elsewhere: RCSB PDB 3SYI · PDBe 3SYI · UniProt B7JBP8
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