Research workbench
Crystal structure of the de novo designed fluorinated peptide ALPHA4F3A
Analyse Crystal structure of the de novo designed fluorinated peptide ALPHA4F3A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TWF
- Type
- protein
- Length
- 51 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA4F3A
- Ligands
- ACE, NA
Structure
x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA4F3A | protein | 25 | 88% helix, 0% strand | — |
| B | ALPHA4F3A | protein | 26 | 88% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- NA · Sodium ion · metal · chains B
- PGE · Triethylene glycol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 712 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 3TWF · Crystal structure of the de novo designed fluorinated peptide alpha4F3a · 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 3TWF · PDBe 3TWF
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