Crystal structure of the YFPnano fusion protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 8 Apr 2020.
Explore 6HR1 in 3D Show helices and sheets RCSB PDB PDBe
6HR1 contains 31 α-helices and 36 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -33-6 | 40 | |
| β-strand | 11-22 | 12 | 1 |
| β-strand | 25-36 | 12 | 1 |
| β-strand | 41-48 | 8 | 1 |
| α-helix | 57-60 | 4 | |
| α-helix | 69-71 | 3 | |
| β-strand | 73 | 1 | 1 |
| α-helix | 76-81 | 6 | |
| α-helix | 83-86 | 4 | |
| β-strand | 92-100 | 9 | 1 |
| β-strand | 105-115 | 11 | 1 |
| β-strand | 118-128 | 11 | 1 |
| β-strand | 141 | 1 | 2 |
| β-strand | 148-155 | 8 | 1 |
| β-strand | 160-170 | 11 | 1 |
| β-strand | 171 | 1 | 2 |
| β-strand | 176-187 | 12 | 1 |
| α-helix | 196-197 | 2 | |
| β-strand | 199-208 | 10 | 1 |
| β-strand | 217-227 | 11 | 1 |
| α-helix | 258-271 | 14 | |
| β-strand | 278-279 | 2 | 3 |
| α-helix | 281-290 | 10 | |
| α-helix | 297-307 | 11 | |
| β-strand | 315-316 | 2 | 3 |
| α-helix | 317-325 | 9 | |
| α-helix | 326-328 | 3 | |
| α-helix | 333-344 | 12 | |
| β-strand | 351-352 | 2 | 4 |
| α-helix | 354-364 | 11 | |
| α-helix | 370-380 | 11 | |
| β-strand | 388-389 | 2 | 4 |
| α-helix | 390-397 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | -34-1 | 36 | |
| α-helix | 4-8 | 5 | |
| β-strand | 11-22 | 12 | 5 |
| β-strand | 25-36 | 12 | 5 |
| β-strand | 41-48 | 8 | 5 |
| α-helix | 57-60 | 4 | |
| α-helix | 69-71 | 3 | |
| β-strand | 73 | 1 | 5 |
| α-helix | 76-81 | 6 | |
| α-helix | 83-86 | 4 | |
| β-strand | 92-100 | 9 | 5 |
| β-strand | 105-115 | 11 | 5 |
| β-strand | 118-128 | 11 | 5 |
| β-strand | 141 | 1 | 6 |
| β-strand | 148-155 | 8 | 5 |
| α-helix | 156-158 | 3 | |
| β-strand | 160-170 | 11 | 5 |
| β-strand | 171 | 1 | 6 |
| β-strand | 176-187 | 12 | 5 |
| α-helix | 194-197 | 4 | |
| β-strand | 199-208 | 10 | 5 |
| β-strand | 217-227 | 11 | 5 |
| α-helix | 258-271 | 14 | |
| β-strand | 278-279 | 2 | 7 |
| α-helix | 281-290 | 10 | |
| α-helix | 297-307 | 11 | |
| β-strand | 315-316 | 2 | 7 |
| α-helix | 317-323 | 7 | |
| α-helix | 333-344 | 12 | |
| β-strand | 351-352 | 2 | 8 |
| α-helix | 354-364 | 11 | |
| α-helix | 370-380 | 11 | |
| β-strand | 388-389 | 2 | 8 |
| α-helix | 390-397 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin light chain kinase 2, skeletal/cardiac muscle,Unconventional myosin-X,Green fluorescent… | A, B | protein | 434 | Oryctolagus cuniculus, Bos taurus, Aequorea victoria, Homo sapiens | P07313 (AlphaFold model), P0DP23 (AlphaFold model), P42212 (AlphaFold model), P79114 (AlphaFold model) |
>6HR1_1 Myosin light chain kinase 2, skeletal/cardiac muscle,Unconventional myosin-X,Green fluorescent protein,Calmodulin-1 (chains A, B) GPHMARWKKAFIAVSAANRFKKISSEEEKRKREEEEVSKGEELFTGVVPILVELDGDVNG HKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFGYGLQCFARYPDHMKQHDFF KSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYN YNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSYQ SALSKDPNEKRDHMVLLEFVTAAGITLGMDELYKGENLYFQSGGSAAAADQLTEEQIAEF KEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMM ARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDG DGQVNYEEFVQMMTAK
Water and common crystallization additives (NA, GOL, EDO) are not listed.
Chimeric single alpha-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology. Collu, G., Bierig, T., Krebs, A.S. et al. Structure (2021). DOI 10.1016/j.str.2021.09.002 · PubMed
Other PDB entries of the same protein (UniProt P07313 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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