Research workbench
Tetramerization and cooperativity in plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
Analyse Tetramerization and cooperativity in plasmodium falciparum glutathione… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FRC
- Type
- protein
- Length
- 404 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- Q8MU52
- Ligands
- 0HG
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 201 | 58% helix, 9% strand | Q8MU52 |
| B | Glutathione S-transferase (EC 2.5.1.18) | protein | 203 | 57% helix, 9% strand | Q8MU52 |
Ligands and binding sites
- 0HG · N-[(4S)-4-ammonio-4-carboxybutanoyl]-S-(4-bromobenzyl)-L-cysteinylglycine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 772 | 0.73 | 0.78 | 75 | 0HG |
| 2 | 94 | 0.60 | 0.87 | 19 | empty |
| 3 | 106 | 0.47 | 0.80 | 17 | empty |
| 4 | 108 | 0.45 | 0.78 | 15 | empty |
| 5 | 53 | 0.28 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1544 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 3FRC · 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 3FRC · PDBe 3FRC · UniProt Q8MU52
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