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Structure of wt human glutathione transferase in complex with cisplatin in the presence of glutathione.
Analyse Structure of wt human glutathione transferase in complex with cisplatin in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DJL
- 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
- GSH, PT, CA, CO3, SO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase P (EC 2.5.1.18) | protein | 210 | 62% helix, 8% strand | P09211 |
| B | Glutathione S-transferase P (EC 2.5.1.18) | protein | 209 | 61% helix, 9% strand | P09211 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
- PT · Platinum (II) ion · metal · 3 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains B
- CO3 · Carbonate ion · ion · chains B
- SO4 · Sulfate 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
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 | 690 | 0.72 | 0.79 | 88 | PT, GSH |
| 2 | 101 | 0.38 | 0.75 | 18 | empty |
| 3 | 64 | 0.32 | 0.75 | 14 | empty |
| 4 | 63 | 0.29 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1300 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 5DJL · Structure of WT Human Glutathione Transferase in complex with cisplatin in the presence… · 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 5DJL · PDBe 5DJL · UniProt P09211
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