Research workbench
Reduced soxax complex from rhodovulum sulfidophilum
Analyse Reduced soxax complex from rhodovulum sulfidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H32
- Type
- protein
- Length
- 395 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diheme cytochrome C; Cytochrome C
- UniProt
- Q939U1, Q939U4
- Ligands
- HEC
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diheme cytochrome C | protein | 261 | 41% helix, 13% strand | Q939U1 |
| B | Cytochrome C | protein | 134 | 32% helix, 4% strand | Q939U4 |
Ligands and binding sites
- HEC · Heme C · ligand · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 824 | 0.82 | 0.85 | 84 | EDO, HEC |
| 2 | 118 | 0.63 | 0.87 | 19 | HEC |
Interfaces
1 interface between chains.
- A–B · 1290 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 cofactor, 1 modified (heme c attachment, oxidation).
Compared structures
- 1H32 · Reduced SoxAX complex from Rhodovulum sulfidophilum · the same entry in another collection · chain A against A, TM-score 1.00
- Q939U1 · AlphaFold monomer V2.0 prediction for L-cysteine S-thiosulfotransferase subunit soxa… · a predicted model of the same protein · 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 Q939U1
- Every structure of UniProt Q939U4
- Elsewhere: RCSB PDB 1H32 · PDBe 1H32 · UniProt Q939U1 · UniProt Q939U4
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