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Crystal structure of human glutathione S-transferase P1- 1[V104] complexed with (9R,10R)-9-(S-glutathionyl)-10- hydroxy-9,10-dihydrophenanthrene
Analyse Crystal structure of human glutathione S-transferase P1- 1[V104] complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PGT
- Type
- protein
- Length
- 419 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
- P09211
- Ligands
- GPR, SO4
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 210 | 60% helix, 8% strand | P09211 |
| B | Glutathione S-transferase (EC 2.5.1.18) | protein | 209 | 61% helix, 9% strand | P09211 |
Ligands and binding sites
- GPR · (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 686 | 0.74 | 0.80 | 82 | GPR |
| 2 | 60 | 0.33 | 0.76 | 10 | empty |
| 3 | 70 | 0.33 | 0.75 | 15 | empty |
| 4 | 73 | 0.31 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1289 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2PGT · Crystal structure of human glutathione S-transferase P1-1[V104] complexed with… · 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 P09211
- Elsewhere: RCSB PDB 2PGT · PDBe 2PGT · UniProt P09211
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