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Structure of glutathione-S-transferase mutant, R21L, from schistosoma haematobium
Analyse Structure of glutathione-S-transferase mutant, R21L, from schistosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CAI
- Type
- protein
- Length
- 417 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase 28 kda
- EC
- 2.5.1.18
- UniProt
- P30113
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase 28 kda (EC 2.5.1.18) | protein | 208 | 52% helix, 10% strand | P30113 |
| B | Glutathione S-transferase 28 kda (EC 2.5.1.18) | protein | 209 | 54% helix, 9% strand | P30113 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 3 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1085 | 0.80 | 0.81 | 109 | SO4, BME |
| 2 | 65 | 0.41 | 0.80 | 18 | PG4 |
| 3 | 64 | 0.38 | 0.79 | 15 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1123 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2CAI · Structure of Glutathione-S-Transferase mutant, R21L, from Schistosoma Haematobium · the same entry in another collection · chain A against A, TM-score 1.00
- P30113 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 28 kda isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P30113
- Elsewhere: RCSB PDB 2CAI · PDBe 2CAI · UniProt P30113
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