6HR1: YFPnano fusion protein

Crystal structure of the YFPnano fusion protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 8 Apr 2020.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
Oryctolagus cuniculus, Bos taurus, Aequorea victoria
Chains
2
Atoms
6,986
Mol. weight
99.94 kDa
Ligands
CA, TLA
Released
8 Apr 2020

Explore 6HR1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 15 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix-33-640
β-strand11-22121
β-strand25-36121
β-strand41-4881
α-helix57-604
α-helix69-713
β-strand7311
α-helix76-816
α-helix83-864
β-strand92-10091
β-strand105-115111
β-strand118-128111
β-strand14112
β-strand148-15581
β-strand160-170111
β-strand17112
β-strand176-187121
α-helix196-1972
β-strand199-208101
β-strand217-227111
α-helix258-27114
β-strand278-27923
α-helix281-29010
α-helix297-30711
β-strand315-31623
α-helix317-3259
α-helix326-3283
α-helix333-34412
β-strand351-35224
α-helix354-36411
α-helix370-38011
β-strand388-38924
α-helix390-3978
Chain B: 16 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix-34-136
α-helix4-85
β-strand11-22125
β-strand25-36125
β-strand41-4885
α-helix57-604
α-helix69-713
β-strand7315
α-helix76-816
α-helix83-864
β-strand92-10095
β-strand105-115115
β-strand118-128115
β-strand14116
β-strand148-15585
α-helix156-1583
β-strand160-170115
β-strand17116
β-strand176-187125
α-helix194-1974
β-strand199-208105
β-strand217-227115
α-helix258-27114
β-strand278-27927
α-helix281-29010
α-helix297-30711
β-strand315-31627
α-helix317-3237
α-helix333-34412
β-strand351-35228
α-helix354-36411
α-helix370-38011
β-strand388-38928
α-helix390-3978

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin light chain kinase 2, skeletal/cardiac muscle,Unconventional myosin-X,Green fluorescent…A, Bprotein434Oryctolagus cuniculus, Bos taurus, Aequorea victoria, Homo sapiensP07313 (AlphaFold model), P0DP23 (AlphaFold model), P42212 (AlphaFold model), P79114 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>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

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa8
TLAL(+)-tartaric acidC4 H6 O61

Water and common crystallization additives (NA, GOL, EDO) are not listed.

Primary citation

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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