Research workbench
Crystal structure of the PSMALPHA3 peptide mutant L15A forming cross- alpha amyloid-like fibril
Analyse Crystal structure of the PSMALPHA3 peptide mutant L15A forming cross- alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GQ5
- Type
- protein
- Length
- 22 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenol-soluble modulin alpha 3 peptide
- UniProt
- P0C807
Structure
x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenol-soluble modulin alpha 3 peptide | protein | 22 | 82% helix, 0% strand | P0C807 |
Ligands and binding sites
- MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GQ5 · Crystal Structure of the PSMalpha3 Peptide Mutant L15A Forming Cross-Alpha Amyloid-like… · the same entry in another collection · chain A against A, TM-score 1.00
- P0C807 · AlphaFold monomer V2.0 prediction for phenol-soluble modulin alpha 3 peptide (P0C807) · a predicted model of the same protein · chain A against A, TM-score 0.68
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0C807
- Elsewhere: RCSB PDB 6GQ5 · PDBe 6GQ5 · UniProt P0C807
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