Research workbench
Energetics of a hydrogen bond (charged and neutral) and of a cation-pi interaction in apoflavodoxin
Analyse Energetics of a hydrogen bond (charged and neutral) and of a cation-pi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QHE
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (flavodoxin)
- UniProt
- P0A3E0
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (flavodoxin) | protein | 168 | 36% helix, 19% strand | P0A3E0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1QHE · Energetics of a hydrogen bond (charged and neutral) and of a cation-pi interaction in… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A3E0 · AlphaFold monomer V2.0 prediction for flavodoxin (P0A3E0) · a predicted model of the same protein · chain A 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 P0A3E0
- Elsewhere: RCSB PDB 1QHE · PDBe 1QHE · UniProt P0A3E0
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