Research workbench
Diheme soxax
Analyse Diheme soxax in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OA8
- Type
- protein
- Length
- 1,227 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soxa; Soxx
- UniProt
- Q7BQR6, Q7BQR5
- Ligands
- HEC, SO4
- Pockets
- 17 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Soxa | protein | 229 | 43% helix, 12% strand | Q7BQR6 |
| B, D, F | Soxx | protein | 180 | 42% helix, 0% strand | Q7BQR5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 984 | 0.86 | 0.87 | 142 | HEC |
| 2 | 534 | 0.83 | 0.89 | 85 | HEC |
| 3 | 451 | 0.80 | 0.87 | 69 | HEC |
| 4 | 61 | 0.75 | 0.99 | 19 | empty |
| 5 | 59 | 0.73 | 0.98 | 16 | empty |
Interfaces
11 interfaces between chains.
- E–F · 2152 Ų buried · 44 hydrogen bonds · protein-protein
- A–B · 2120 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 2040 Ų buried · 45 hydrogen bonds · protein-protein
- D–E · 353 Ų buried · 7 hydrogen bonds · protein-protein
- D–F · 331 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 cofactor, 6 disulfide, 3 modified (heme c attachment, disulfide, oxidation).
Compared structures
- 3OA8 · Diheme SoxAX · 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 Q7BQR6
- Every structure of UniProt Q7BQR5
- Elsewhere: RCSB PDB 3OA8 · PDBe 3OA8 · UniProt Q7BQR6 · UniProt Q7BQR5
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