MolNFT v1 · #18183 · protein
Crystal structure of human glutathione S-transferase P1- 1[V104] complexed with S-hexylglutathione
1PGT: “Crystal structure of human glutathione S-transferase P1- 1[V104] complexed with S-hexylglutathione”. X-ray diffraction, 1 ligand (GTX), 4 pockets (best druggability 0.73). MolNFT v1 #18183 on GenesisL1: 3D structure, binding sites…
- PDB
- 1PGT
- 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
- GTX
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 210 | 63% helix, 8% strand | P09211 |
| B | Glutathione S-transferase (EC 2.5.1.18) | protein | 209 | 61% helix, 9% strand | P09211 |
Ligands and binding sites
- GTX · S-hexylglutathione · ligand · 2 copies · chains A, B
- 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 | 680 | 0.73 | 0.79 | 84 | GTX |
| 2 | 81 | 0.37 | 0.76 | 17 | empty |
| 3 | 86 | 0.37 | 0.75 | 14 | empty |
| 4 | 72 | 0.30 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1306 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1PGT · 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 1PGT · PDBe 1PGT · UniProt P09211
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