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Structure of R21Q mutant of SH28GST
Analyse Structure of R21Q mutant of SH28GST in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C8U
- Type
- protein
- Length
- 404 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase 28 kda
- EC
- 2.5.1.18
- UniProt
- P30113
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione S-transferase 28 kda (EC 2.5.1.18) | protein | 202 | 55% helix, 10% strand | P30113 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1154 | 0.78 | 0.80 | 100 | SO4, BME |
| 2 | 142 | 0.46 | 0.77 | 34 | empty |
| 3 | 67 | 0.37 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1166 Ų buried · 10 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 P30113
- Elsewhere: RCSB PDB 2C8U · PDBe 2C8U · UniProt P30113
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