6BWZ: SYSGYS peptide from low-complexity domain of FUS
SYSGYS from low-complexity domain of FUS, residues 37-42. Determined by X-ray diffraction at 1.1 Å resolution. Released 4 Apr 2018.
- Method
- X-ray diffraction
- Resolution
- 1.1 Å
- Organism
- Homo sapiens
- Chains
- 1
- Atoms
- 48
- Mol. weight
- 0.66 kDa
- Released
- 4 Apr 2018
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RCSB PDB
PDBe
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| SYSGYS peptide from low-complexity domain of FUS | A | protein | 6 | Homo sapiens | P35637 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>6BWZ_1 SYSGYS peptide from low-complexity domain of FUS (chains A)
SYSGYS
Primary citation
Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks. Hughes, M.P., Sawaya, M.R., Boyer, D.R. et al. Science (2018) 359:698-701. DOI 10.1126/science.aan6398 · PubMed
Other PDB entries of the same protein (UniProt P35637 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6KJ3 0.6 Å, 120kV MicroED structure of FUS (37-42) SYSGYS solved from merged datasets at 0.60 A
- 6KJ1 0.65 Å, 200kV MicroED structure of FUS (37-42) SYSGYS solved from merged datasets at 0.65 A
- 6KJ4 0.65 Å, 120kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.65 A
- 6KJ2 0.67 Å, 200kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.67 A
- 5XSG 0.73 Å, Ultrahigh resolution structure of FUS (37-42) SYSGYS determined by MicroED
- 6BXV 1.1 Å, SYSSYGQS from low-complexity domain of FUS, residues 54-61
- 6BZP 1.1 Å, STGGYG from low-complexity domain of FUS, residues 77-82
- 5XRR 1.5 Å, Crystal structure of FUS (54-59) SYSSYG
- 4FDD 2.3 Å, Crystal structure of KAP beta2-PY-NLS
- 6XFM 2.62 Å, Molecular structure of the core of amyloid-like fibrils formed by residues 111-214 of FUS
- 7CYL 2.7 Å, Crystal structure of Karyopherin-beta2 in complex with FUS PY-NLS(P525L)
- 5YVI 2.9 Å, Crystal structure of Karyopherin beta2 in complex with FUS(456-526)
Browse structure collections
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