MolNFT v1 · #57860 · protein
Designed peptide alpha-1, racemic P1BAR form
3AL1 · Protein (D, L-alpha-1): “Designed peptide alpha-1, racemic P1BAR form”. X-ray diffraction, 2 ligands (ACE, ETA). MolNFT v1 #57860 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3AL1
- Type
- protein
- Length
- 24 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (D, L-alpha-1)
- Ligands
- ACE, ETA
Structure
x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (D, L-alpha-1) | protein | 12 | 83% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- ETA · Ethanolamine · ligand · 2 copies · chains B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 311 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3AL1 · Designed peptide alpha-1, racemic P1BAR form · 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 3AL1 · PDBe 3AL1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.