Research workbench
Crystal structure of thioredoxin reductase 2 from staphylococcus aureus
Analyse Crystal structure of thioredoxin reductase 2 from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A4J
- Type
- protein
- Length
- 678 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin--NADP reductase
- EC
- 1.18.1.2
- UniProt
- A0A1Q4GXS1
- Ligands
- FAD
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 340 | 27% helix, 26% strand | A0A1Q4GXS1 |
| B | Ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 338 | 27% helix, 26% strand | A0A1Q4GXS1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 574 | 0.78 | 0.84 | 64 | FAD |
| 2 | 608 | 0.77 | 0.83 | 76 | FAD |
| 3 | 102 | 0.65 | 0.90 | 28 | empty |
| 4 | 111 | 0.63 | 0.88 | 26 | empty |
| 5 | 142 | 0.45 | 0.77 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 3039 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6A4J · Crystal structure of Thioredoxin reductase 2 from Staphylococcus aureus · 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 A0A1Q4GXS1
- Elsewhere: RCSB PDB 6A4J · PDBe 6A4J · UniProt A0A1Q4GXS1
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