Research workbench
NMR solution structure and model membrane interaction studies of the peptide hylin A1 from the arboreal south american frog hypsiboas albopunctatus
Analyse NMR solution structure and model membrane interaction studies of the peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N0O
- Type
- protein
- Length
- 18 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hylin-A1
- UniProt
- P85982
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hylin-A1 | protein | 18 | 89% helix, 0% strand | P85982 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2N0O · NMR Solution Structure and Model Membrane Interaction Studies of the Peptide Hylin a1… · the same entry in another collection · chain A against A, TM-score 1.00
- P85982 · AlphaFold monomer V2.0 prediction for hylin-A1 (P85982) · a predicted model of the same protein · chain A against A, TM-score 0.51
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 P85982
- Elsewhere: RCSB PDB 2N0O · PDBe 2N0O · UniProt P85982
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