Research workbench
The 2.4 ångström structure of the fasciola hepatica mu class GST, GST26
Analyse The 2.4 ångström structure of the fasciola hepatica mu class GST, GST26 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WRT
- Type
- protein
- Length
- 2,604 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase class-mu 26 kda isozyme 51
- EC
- 2.5.1.18
- UniProt
- P30112
- Ligands
- CL
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Glutathione S-transferase class-mu 26 kda isozyme 51 (EC 2.5.1.18) | protein | 217 | 50% helix, 10% strand | P30112 |
Ligands and binding sites
- CL · Chloride ion · ion · 12 copies · chains A, B, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1057 | 0.81 | 0.82 | 114 | empty |
| 2 | 956 | 0.80 | 0.82 | 94 | CL |
| 3 | 1110 | 0.78 | 0.80 | 93 | CL |
| 4 | 1155 | 0.78 | 0.80 | 102 | empty |
| 5 | 873 | 0.77 | 0.80 | 75 | CL |
Interfaces
19 interfaces between chains.
- A–B · 1444 Ų buried · 14 hydrogen bonds · protein-protein
- K–L · 1418 Ų buried · 13 hydrogen bonds · protein-protein
- G–H · 1416 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 1389 Ų buried · 11 hydrogen bonds · protein-protein
- I–J · 1349 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2WRT · The 2.4 Angstrom structure of the Fasciola hepatica mu class GST, GST26 · the same entry in another collection · chain L against L, 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 P30112
- Elsewhere: RCSB PDB 2WRT · PDBe 2WRT · UniProt P30112
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