Research workbench
Tetrathionate hydrolase from acidithiobacillus ferrooxidans mutant - D325N
Analyse Tetrathionate hydrolase from acidithiobacillus ferrooxidans mutant - D325N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CQY
- Type
- protein
- Length
- 2,630 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B7J3C9
- Ligands
- SO4
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 425 | — | B7J3C9 |
| B | — | protein | 436 | — | B7J3C9 |
| C | — | protein | 409 | — | B7J3C9 |
| D | — | protein | 464 | — | B7J3C9 |
| E | — | protein | 451 | — | B7J3C9 |
| F | — | protein | 445 | — | B7J3C9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CQY · Tetrathionate hydrolase from Acidithiobacillus ferrooxidans mutant - D325N · 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 B7J3C9
- Elsewhere: RCSB PDB 7CQY · PDBe 7CQY · UniProt B7J3C9
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