Research workbench
The crystal structure of the GLUTAREDOXIN(GRX-1) from archaeoglobus fulgidus
Analyse The crystal structure of the GLUTAREDOXIN(GRX-1) from archaeoglobus fulgidus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IC4
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaredoxin (grx-1)
- UniProt
- O28736
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaredoxin (grx-1) | protein | 92 | 43% helix, 17% strand | O28736 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3IC4 · The crystal structure of the glutaredoxin(grx-1) from Archaeoglobus fulgidus · 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
- Every structure of UniProt O28736
- Elsewhere: RCSB PDB 3IC4 · PDBe 3IC4 · UniProt O28736
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