Research workbench
Crystal structure of a tau class GST mutant from glycine
Analyse Crystal structure of a tau class GST mutant from glycine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AGY
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- O49235
- Ligands
- 4NM, GTB, PO4
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 219 | 60% helix, 9% strand | O49235 |
| B | Glutathione S-transferase (EC 2.5.1.18) | protein | 217 | 61% helix, 9% strand | O49235 |
Ligands and binding sites
- 4NM · 4-nitrophenyl methanethiol · ligand · 3 copies · chains A, B
- GTB · S-(P-nitrobenzyl)glutathione · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 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 | 814 | 0.77 | 0.80 | 76 | 4NM, GTB, PO4 |
| 2 | 148 | 0.47 | 0.77 | 31 | empty |
| 3 | 57 | 0.35 | 0.78 | 19 | empty |
| 4 | 59 | 0.32 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1138 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5AGY · Crystal structure of a tau class GST mutant from glycine · 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 O49235
- Elsewhere: RCSB PDB 5AGY · PDBe 5AGY · UniProt O49235
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