MolNFT v1 · #64017 · protein
Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
3FR3: “Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic…”. X-ray diffraction. MolNFT v1 #64017 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FR3
- Type
- protein
- Length
- 398 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8MU52
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 201 | — | Q8MU52 |
| B | — | protein | 197 | — | Q8MU52 |
Compared structures
- 3FR3 · Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are… · 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 Q8MU52
- Elsewhere: RCSB PDB 3FR3 · PDBe 3FR3 · UniProt Q8MU52
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.