Research workbench
Crystal structure of the holo form of glutaredoxin C5 from arabidopsis thaliana
Analyse Crystal structure of the holo form of glutaredoxin C5 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RHC
- Type
- protein
- Length
- 203 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin-C5, chloroplastic
- UniProt
- Q8GWS0
- Ligands
- GSH, FES
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaredoxin-C5, chloroplastic | protein | 103 | 54% helix, 15% strand | Q8GWS0 |
| B | Glutaredoxin-C5, chloroplastic | protein | 100 | 52% helix, 17% strand | Q8GWS0 |
Ligands and binding sites
- GSH · Glutathione · ligand · 2 copies · chains A, B
- FES · Fe2/s2 (inorganic) cluster · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.50 | 0.81 | 17 | GSH, FES |
Interfaces
1 interface between chains.
- A–B · 193 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3RHC · Crystal structure of the holo form of glutaredoxin C5 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
- Q8GWS0 · AlphaFold monomer V2.0 prediction for glutaredoxin-C5, chloroplastic (Q8GWS0) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q8GWS0
- Elsewhere: RCSB PDB 3RHC · PDBe 3RHC · UniProt Q8GWS0
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