Research workbench
Sulfite dehydrogenase from starkeya novella mutant
Analyse Sulfite dehydrogenase from starkeya novella mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CA4
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SULFITE\:CYTOCHROME C oxidoreductase subunit a; SULFITE\:CYTOCHROME C oxidoreductase…
- UniProt
- Q9LA16, Q9LA15
- Ligands
- MSS, HEC
- Pockets
- 6 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SULFITE\:CYTOCHROME C oxidoreductase subunit a | protein | 373 | 10% helix, 39% strand | Q9LA16 |
| B | SULFITE\:CYTOCHROME C oxidoreductase subunit B | protein | 81 | 49% helix, 2% strand | Q9LA15 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.80 | 0.85 | 73 | HEC |
| 2 | 91 | 0.76 | 0.97 | 21 | MSS |
| 3 | 194 | 0.51 | 0.77 | 26 | empty |
| 4 | 102 | 0.43 | 0.78 | 29 | empty |
| 5 | 117 | 0.43 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1400 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).
Compared structures
- 2CA4 · Sulfite dehydrogenase from Starkeya Novella mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9LA16
- Every structure of UniProt Q9LA15
- Elsewhere: RCSB PDB 2CA4 · PDBe 2CA4 · UniProt Q9LA16 · UniProt Q9LA15
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