Research workbench
Structure of yeast GRX2-C30S mutant with glutathionyl mixed disulfide
Analyse Structure of yeast GRX2-C30S mutant with glutathionyl mixed disulfide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D5J
- Type
- protein
- Length
- 219 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin-2, mitochondrial
- UniProt
- P17695
- Ligands
- GSH
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaredoxin-2, mitochondrial | protein | 112 | 58% helix, 16% strand | P17695 |
| B | Glutaredoxin-2, mitochondrial | protein | 107 | 55% helix, 17% strand | P17695 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.37 | 0.74 | 21 | GSH |
Interfaces
1 interface between chains.
- A–B · 427 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 P17695
- Elsewhere: RCSB PDB 3D5J · PDBe 3D5J · UniProt P17695
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