4R0U: Alpha-synuclein
Tgvtava, an amyloid forming segment from alpha synuclein, residues 72-78. Determined by X-ray diffraction at 1.38 Å resolution. Released 17 Dec 2014.
- Method
- X-ray diffraction
- Resolution
- 1.38 Å
- Organism
- Homo sapiens
- Chains
- 1
- Atoms
- 50
- Mol. weight
- 0.62 kDa
- Released
- 17 Dec 2014
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RCSB PDB
PDBe
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Alpha-synuclein | A | protein | 7 | Homo sapiens | P37840 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>4R0U_1 Alpha-synuclein (chains A)
TGVTAVA
Primary citation
Structure-based design of functional amyloid materials. Li, D., Jones, E.M., Sawaya, M.R. et al. J Am Chem Soc (2014) 136:18044-18051. DOI 10.1021/ja509648u · PubMed
Other PDB entries of the same protein (UniProt P37840 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8JJV 1.23 Å, Structure of truncated form of nanobody in complex with alpha-synuclein peptide
- 8JLY 1.29 Å, Structure of nanobody in complex with alpha-synuclein peptide
- 3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
- 6I42 1.38 Å, Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex
- 4ZNN 1.41 Å, MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of…
- 4RIL 1.43 Å, Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of…
- 4R0W 1.5 Å, Vvtgvta, an amyloid forming segment from alpha synuclein, residues 70-76
- 3Q26 1.54 Å, Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (MBP)
- 3Q28 1.6 Å, Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)
- 5CRW 1.6 Å, Crystal structure of the b'-a' domain of oxidized protein disulfide isomerase complexed…
- 2X6M 1.62 Å, Structure of a single domain camelid antibody fragment in complex with a C-terminal…
- 8OG0 1.71 Å, Crystal structure of MJF14-6-4-2 Fab fragment in complex with epitope peptide
Browse structure collections
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