Research workbench
Crystal structure of alamethicin at 1.5 ångström resolution
Analyse Crystal structure of alamethicin at 1.5 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AMT
- Type
- protein
- Length
- 60 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alamethicin F30
- Ligands
- ACE, CCN
Structure
x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Alamethicin F30 | protein | 20 | 80% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, B, C
- CCN · Acetonitrile · ligand · 2 copies · chains A, C, B
- MOH · Methanol · additive · 13 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
2 interfaces between chains.
- A–C · 333 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 259 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 27 modified, 3 covalent (nonstandard, covalent ligand).
Compared structures
- 1AMT · Crystal structure of alamethicin at 1.5 angstrom resolution · 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 1AMT · PDBe 1AMT
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