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Crystal structure of mouse glutathione S-transferase, MU7 (GSTM7) at 1.6 a resolution
Analyse Crystal structure of mouse glutathione S-transferase, MU7 (GSTM7) at 1.6 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DC5
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase, mu 7
- EC
- 2.5.1.18
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase, mu 7 (EC 2.5.1.18) | protein | 218 | 51% helix, 10% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1016 | 0.73 | 0.76 | 79 | empty |
| 2 | 84 | 0.47 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1440 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 2DC5 · Crystal structure of mouse glutathione S-transferase, mu7 (GSTM7) at 1.6 A resolution · 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
- Elsewhere: RCSB PDB 2DC5 · PDBe 2DC5
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