Research workbench
De novo-designed and disulfide-bridged peptide heterodimer - HD2
Analyse De novo-designed and disulfide-bridged peptide heterodimer - HD2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FBA
- Type
- protein
- Length
- 24 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glu-cys-arg-glu-tyr-gly-pro-LE1-lys-LE1-LE1-ala-NH2…
- Ligands
- NH2
Structure
solution nmr · 2 distinct chains · 0% helix, 67% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glu-cys-arg-glu-tyr-gly-pro-LE1-lys-LE1-LE1-ala-NH2 | protein | 12 | 0% helix, 67% strand | — |
| B | Ala-LE1-cys-glu-cys-gly-pro-thr-arg-glu-cys-lys-NH2 | protein | 12 | 0% helix, 67% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · 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 · 235 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 7FBA · De Novo-Designed and Disulfide-Bridged Peptide Heterodimer - hd2 · the same entry in another collection · chain B against B, 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 7FBA · PDBe 7FBA
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