Research workbench
Structure of beta-purothionin at room temperature and 1.7 ångströms resolution
Analyse Structure of beta-purothionin at room temperature and 1.7 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BHP
- Type
- protein
- Length
- 45 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-purothionin
- UniProt
- P01543
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-purothionin | protein | 45 | 38% helix, 13% strand | P01543 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1BHP · Structure of beta-purothionin at room temperature and 1.7 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P01543 · AlphaFold monomer V2.0 prediction for purothionin a-1 (P01543) · 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 P01543
- Elsewhere: RCSB PDB 1BHP · PDBe 1BHP · UniProt P01543
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.