Research workbench
Crystal structure of human glutathione transferase theta-2, complex with inorganic phosphate, gsh free, target efi-507257
Analyse Crystal structure of human glutathione transferase theta-2, complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MPF
- Type
- protein
- Length
- 491 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase theta-2
- EC
- 2.5.1.18
- UniProt
- P0CG29
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase theta-2 (EC 2.5.1.18) | protein | 243 | 58% helix, 8% strand | P0CG29 |
| B | Glutathione S-transferase theta-2 (EC 2.5.1.18) | protein | 248 | 59% helix, 7% strand | P0CG29 |
Ligands and binding sites
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 | 993 | 0.89 | 0.91 | 108 | PO4 |
| 2 | 51 | 0.33 | 0.78 | 20 | empty |
| 3 | 65 | 0.32 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1593 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4MPF · Crystal structure of human glutathione transferase theta-2, complex with inorganic… · the same entry in another collection · chain A against A, TM-score 1.00
- P0CG29 · AlphaFold monomer V2.0 prediction for glutathione S-transferase theta-2 (P0CG29) · 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 P0CG29
- Elsewhere: RCSB PDB 4MPF · PDBe 4MPF · UniProt P0CG29
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