MolNFT v1 · #46634 · protein
Structure of glutathione-S-transferase C169A mutant
2OAD · Glutathione S-transferase P 1: “Structure of glutathione-S-transferase C169A mutant”. X-ray diffraction, 1 ligand (GTB), 5 pockets (best druggability 0.72). MolNFT v1 #46634 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2OAD
- 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
- 5 · best druggability 0.72
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
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.72 | 0.78 | 81 | GTB |
| 2 | 117 | 0.39 | 0.75 | 19 | empty |
| 3 | 108 | 0.37 | 0.74 | 20 | empty |
| 4 | 58 | 0.34 | 0.78 | 18 | empty |
| 5 | 53 | 0.29 | 0.75 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1335 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
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 2OAD · PDBe 2OAD · UniProt P19157
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.