Research workbench
HYEN D
Analyse HYEN D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RIH
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-[I11L]HYEN D; Cyclotide hyen-D
- UniProt
- C0HLN8
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-[I11L]HYEN D | protein | 30 | 17% helix, 43% strand | — |
| B | Cyclotide hyen-D | protein | 30 | 17% helix, 43% strand | C0HLN8 |
Ligands and binding sites
- FLC · Citrate anion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 30 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 d-amino, 6 disulfide (D-amino acid, disulfide).
Compared structures
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 C0HLN8
- Elsewhere: RCSB PDB 7RIH · PDBe 7RIH · UniProt C0HLN8
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