Research workbench
Crystal structure of sjtgr (thioredoxin glutathione reductase from schistosoma JAPONICUMI)COMPLEX with FAD
Analyse Crystal structure of sjtgr (thioredoxin glutathione reductase from schistosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LA1
- Type
- protein
- Length
- 1,172 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin glutathione reductase
- EC
- 1.6.4.5
- UniProt
- B5THG7
- Ligands
- FAD
- Pockets
- 14 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thioredoxin glutathione reductase (EC 1.6.4.5) | protein | 586 | 37% helix, 25% strand | B5THG7 |
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
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 511 | 0.86 | 0.92 | 54 | empty |
| 2 | 976 | 0.82 | 0.84 | 110 | FAD |
| 3 | 909 | 0.81 | 0.83 | 103 | FAD |
| 4 | 1135 | 0.76 | 0.78 | 80 | empty |
| 5 | 866 | 0.73 | 0.78 | 66 | empty |
Interfaces
1 interface between chains.
- A–B · 3543 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4LA1 · Crystal structure of SjTGR (thioredoxin glutathione reductase from Schistosoma… · 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 B5THG7
- Elsewhere: RCSB PDB 4LA1 · PDBe 4LA1 · UniProt B5THG7
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