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Crystal structure of murine alpha-class GSTA4-4
Analyse Crystal structure of murine alpha-class GSTA4-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GUK
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase A4-4
- EC
- 2.5.1.18
- UniProt
- P24472
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 56% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase A4-4 (EC 2.5.1.18) | protein | 215 | 57% helix, 7% strand | P24472 |
| B | Glutathione S-transferase A4-4 (EC 2.5.1.18) | protein | 209 | 55% helix, 7% strand | P24472 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 747 | 0.69 | 0.76 | 57 | empty |
| 2 | 59 | 0.55 | 0.88 | 18 | empty |
| 3 | 56 | 0.53 | 0.88 | 19 | empty |
| 4 | 138 | 0.45 | 0.77 | 28 | empty |
| 5 | 107 | 0.37 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1318 Ų buried · 5 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 P24472
- Elsewhere: RCSB PDB 1GUK · PDBe 1GUK · UniProt P24472
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