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Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability
Analyse Connecting hydrophobic surfaces in cyclic peptides increases membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L98
- Type
- protein
- Length
- 5 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic peptide ala-mea-pro-ile-pro-itz
- Ligands
- ITZ
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic peptide ala-mea-pro-ile-pro-itz | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- ITZ · 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 7L98 · Connecting hydrophobic surfaces in cyclic peptides increases membrane permeability · 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
- Elsewhere: RCSB PDB 7L98 · PDBe 7L98
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