Research workbench
Crystal structure of glutathione transferase pi in complex with S-nitrosoglutathione
Analyse Crystal structure of glutathione transferase pi in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A2R
- Type
- protein
- Length
- 419 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase P
- EC
- 2.5.1.18
- UniProt
- P09211
- Ligands
- GSN, CA, CO3
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase P (EC 2.5.1.18) | protein | 210 | 62% helix, 9% strand | P09211 |
| B | Glutathione S-transferase P (EC 2.5.1.18) | protein | 209 | 61% helix, 9% strand | P09211 |
Ligands and binding sites
- GSN · 2-amino-5-[1-(carboxylatomethylcarbamoyl)-2-nitrososulfanyl-ethyl]amino-5-oxo-pentanoate · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · chains B
- CO3 · Carbonate ion · ion · chains B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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 | 600 | 0.72 | 0.79 | 74 | GSN |
| 2 | 98 | 0.38 | 0.75 | 19 | empty |
| 3 | 60 | 0.36 | 0.78 | 17 | empty |
| 4 | 67 | 0.32 | 0.75 | 16 | empty |
| 5 | 64 | 0.30 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1305 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2A2R · Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione · the same entry in another collection · chain A against A, TM-score 1.00
- P09211 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P (P09211) · a predicted model of the same protein · chain B 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 2A2R · PDBe 2A2R · UniProt P09211
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