MolNFT v1 · #909 · protein
Crystal structure of ALPHA1: implications for protein design
1AL1 · Alpha helix peptide: ellkklleelkg: “Crystal structure of ALPHA1: implications for protein design”. X-ray diffraction, 2 ligands (ACE, SO4). MolNFT v1 #909 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AL1
- Type
- protein
- Length
- 12 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha helix peptide: ellkklleelkg
- Ligands
- ACE, SO4
Structure
x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha helix peptide: ellkklleelkg | protein | 12 | 67% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1AL1 · Crystal structure of ALPHA1: implications for protein design · 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 1AL1 · PDBe 1AL1
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