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Thioredoxin glutathione reductase from schistosoma mansoni in complex with 1,8-naphthyridine-2-carboxylic acid
Analyse Thioredoxin glutathione reductase from schistosoma mansoni in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FP4
- Type
- protein
- Length
- 587 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G4V8J4
- Ligands
- FAD, E1T, 250, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 587 | — | G4V8J4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- E1T · 1,8-naphthyridine-2-carboxylic acid · ligand · chains A
- 250 · (2R)-2-hydroxy-3-[4-(2-hydroxyethyl)piperazin-1-yl]propane-1-sulfonic acid · ligand · chains A
- NA · Sodium ion · metal · chains A
- PGE · Triethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FP4 · Thioredoxin glutathione reductase from Schistosoma mansoni in complex with… · 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 G4V8J4
- Elsewhere: RCSB PDB 6FP4 · PDBe 6FP4 · UniProt G4V8J4
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