MolNFT v1 · #191101 · protein
Crystal structure of poplar glutathione transferase U19
7ZS3: “Crystal structure of poplar glutathione transferase U19”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #191101 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7ZS3
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase
- EC
- 2.5.1.18
- UniProt
- B9HKX9
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase (EC 2.5.1.18) | protein | 215 | 57% helix, 9% strand | B9HKX9 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A
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 | 249 | 0.65 | 0.82 | 31 | empty |
| 2 | 125 | 0.39 | 0.74 | 19 | empty |
| 3 | 61 | 0.33 | 0.76 | 12 | ACT |
| 4 | 55 | 0.32 | 0.77 | 19 | ACT |
Compared structures
- 7ZS3 · Crystal structure of poplar glutathione transferase U19 · 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 B9HKX9
- Elsewhere: RCSB PDB 7ZS3 · PDBe 7ZS3 · UniProt B9HKX9
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