Research workbench
Crystal structure of the proline-rich lasso peptide caulosegnin II
Analyse Crystal structure of the proline-rich lasso peptide caulosegnin II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D9E
- Type
- protein
- Length
- 19 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caulosegnin II
- UniProt
- D5VKJ8
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caulosegnin II | protein | 19 | 0% helix, 26% strand | D5VKJ8 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 5D9E · Crystal Structure of the Proline-rich Lasso Peptide Caulosegnin II · the same entry in another collection · chain A against A, TM-score 1.00
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 D5VKJ8
- Elsewhere: RCSB PDB 5D9E · PDBe 5D9E · UniProt D5VKJ8
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