Research workbench
Human glutathione-S-transferase T1-1 W234R mutant, complex with S- hexylglutathione
Analyse Human glutathione-S-transferase T1-1 W234R mutant, complex with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C3Q
- Type
- protein
- Length
- 956 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase theta 1
- EC
- 2.5.1.18
- UniProt
- P30711
- Ligands
- GTX, IOD
- Pockets
- 7 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Glutathione S-transferase theta 1 (EC 2.5.1.18) | protein | 239 | 62% helix, 7% strand | P30711 |
Ligands and binding sites
- GTX · S-hexylglutathione · ligand · 4 copies · chains A, B, C, D
- IOD · Iodide ion · ion · 31 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1038 | 0.89 | 0.90 | 95 | GTX, IOD |
| 2 | 583 | 0.84 | 0.89 | 59 | IOD, GTX |
| 3 | 517 | 0.83 | 0.89 | 47 | GTX, IOD |
| 4 | 944 | 0.77 | 0.79 | 101 | IOD |
| 5 | 113 | 0.44 | 0.78 | 22 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1504 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1481 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 388 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 121 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 90 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2C3Q · Human glutathione-S-transferase T1-1 W234R mutant, complex with S- hexylglutathione · the same entry in another collection · chain B against B, TM-score 1.00
- P30711 · AlphaFold monomer V2.0 prediction for glutathione S-transferase theta-1 (P30711) · a predicted model of the same protein · 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 P30711
- Elsewhere: RCSB PDB 2C3Q · PDBe 2C3Q · UniProt P30711
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