MolNFT v1 · #46633 · protein
Mouse C14A glutathione-S-transferase mutant in complex with S-(P- nitrobenzyl) glutathione
2OAC · Glutathione S-transferase P 1: “Mouse C14A glutathione-S-transferase mutant in complex with S-(P- nitrobenzyl) glutathione”. X-ray diffraction, 1 ligand (GTB), 4 pockets (best druggability 0.73). MolNFT v1 #46633 on GenesisL1: 3D…
- PDB
- 2OAC
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase P 1
- EC
- 2.5.1.18
- UniProt
- P19157
- Ligands
- GTB
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase P 1 (EC 2.5.1.18) | protein | 209 | 60% helix, 8% strand | P19157 |
Ligands and binding sites
- GTB · S-(P-nitrobenzyl)glutathione · ligand · 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 | 698 | 0.73 | 0.79 | 83 | GTB |
| 2 | 91 | 0.36 | 0.75 | 19 | empty |
| 3 | 86 | 0.36 | 0.75 | 20 | empty |
| 4 | 51 | 0.27 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1314 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2OAC · Mouse C14A Glutathione-S-Transferase Mutant in Complex with S-(p-nitrobenzyl) Glutathione · the same entry in another collection · chain A against A, TM-score 1.00
- P19157 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P 1 (P19157) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P19157
- Elsewhere: RCSB PDB 2OAC · PDBe 2OAC · UniProt P19157
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