Research workbench
High resolution structure of high-potential iron-sulfur protein in the reduced state
Analyse High resolution structure of high-potential iron-sulfur protein in the reduced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WQR
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High-potential iron-sulfur protein
- UniProt
- P80176
- Ligands
- SF4, SO4
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High-potential iron-sulfur protein | protein | 83 | 23% helix, 23% strand | P80176 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WQR · High resolution structure of high-potential iron-sulfur protein in the reduced state · the same entry in another collection · chain A against A, TM-score 1.00
- P80176 · AlphaFold monomer V2.0 prediction for high-potential iron-sulfur protein (P80176) · a predicted model of the same protein · chain A 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 P80176
- Elsewhere: RCSB PDB 5WQR · PDBe 5WQR · UniProt P80176
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