Research workbench
Structure of alpha-1-purothionin at room temperature and 2.8 ångströms resolution
Analyse Structure of alpha-1-purothionin at room temperature and 2.8 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PLH
- Type
- protein
- Length
- 45 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1-purothionin
- UniProt
- P01544
- Ligands
- SBT, PO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-purothionin | protein | 45 | 40% helix, 13% strand | P01544 |
Ligands and binding sites
- SBT · 2-butanol · ligand · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- ACT · Acetate ion · additive · 3 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
- 2PLH · Structure of alpha-1-purothionin at room temperature and 2.8 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P01544 · AlphaFold monomer V2.0 prediction for alpha-1-purothionin (P01544) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P01544
- Elsewhere: RCSB PDB 2PLH · PDBe 2PLH · UniProt P01544
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