Research workbench
Crystal structure of desulforedoxin from desulfovibrio gigas at 1.8 a resolution
Analyse Crystal structure of desulforedoxin from desulfovibrio gigas at 1.8 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DXG
- Type
- protein
- Length
- 72 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Desulforedoxin
- UniProt
- P00273
- Ligands
- FE
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Desulforedoxin | protein | 36 | 0% helix, 44% strand | P00273 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 751 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1DXG · Crystal structure of desulforedoxin from desulfovibrio gigas at 1.8 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P00273 · AlphaFold monomer V2.0 prediction for desulforedoxin (P00273) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P00273
- Elsewhere: RCSB PDB 1DXG · PDBe 1DXG · UniProt P00273
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