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Crystal structure of GRX1 in glutathionylated form
Analyse Crystal structure of GRX1 in glutathionylated form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C1S
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin-1
- EC
- 1.20.4.1
- UniProt
- P25373
- Ligands
- GSH
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaredoxin-1 (EC 1.20.4.1) | protein | 107 | 53% helix, 17% strand | P25373 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 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 P25373
- Elsewhere: RCSB PDB 3C1S · PDBe 3C1S · UniProt P25373
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