6WTB: Sort-Tagged Drosophila Cryptochrome

Sort-Tagged Drosophila Cryptochrome. Determined by X-ray diffraction at 2.58 Å resolution. Released 5 May 2021.

Method
X-ray diffraction
Resolution
2.58 Å
Organism
Drosophila melanogaster
Chains
2
Atoms
9,008
Mol. weight
136.85 kDa
Ligands
FAD, MG
Released
5 May 2021

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

Secondary structure: helices and β-sheets

6WTB contains 69 α-helices and 21 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: 35 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand5-1171
α-helix21-266
α-helix27-326
β-strand34-4181
α-helix54-7320
β-strand82-8431
α-helix88-9811
β-strand101-10771
α-helix112-1143
α-helix115-12814
β-strand131-13551
α-helix143-1497
α-helix158-16811
α-helix171-1744
α-helix176-1783
β-strand18511
α-helix190-1956
α-helix202-2043
α-helix205-2084
α-helix227-24721
α-helix252-2554
α-helix267-2726
α-helix277-28812
β-strand29612
β-strand30112
α-helix303-3053
α-helix306-32116
α-helix342-3454
α-helix347-3559
α-helix361-37212
α-helix378-38811
α-helix397-40711
α-helix413-42412
α-helix430-4334
α-helix440-4478
α-helix452-4576
α-helix459-4613
α-helix466-4694
α-helix472-4743
α-helix479-4824
β-strand48713
β-strand49113
α-helix492-4943
α-helix498-51518
α-helix528-5347
Chain B: 34 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand6-1164
α-helix21-266
β-strand35-4174
α-helix46-483
α-helix54-7320
β-strand82-8434
α-helix88-9811
β-strand101-10774
α-helix112-1143
α-helix115-12814
β-strand131-13554
α-helix143-1497
α-helix158-16811
α-helix171-1799
α-helix190-1956
α-helix205-2084
β-strand21315
β-strand21615
α-helix227-24721
α-helix252-2554
α-helix267-2715
α-helix277-28812
β-strand29616
β-strand30116
α-helix303-3053
α-helix306-32116
α-helix326-3294
α-helix342-3443
α-helix347-3548
α-helix361-37212
α-helix378-38811
α-helix398-40710
α-helix413-42412
α-helix430-4334
α-helix440-4478
α-helix452-4576
α-helix459-4613
α-helix466-4683
α-helix472-4743
α-helix477-4826
β-strand48717
β-strand49117
α-helix492-4943
α-helix498-51518
α-helix528-5347

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cryptochrome-1A, Bprotein593Drosophila melanogasterO77059 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6WTB_1 Cryptochrome-1 (chains A, B)
MGSSWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGENLYFQSGGHMMATRGANVIWFRHGL
RLHDNPALLAALADKDQGIALIPVFIFDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAAT
DGRGRLLVFEGEPAYIFRRLHEQVRLHRICIEQDCEPIWNERDESIRSLCRELNIDFVEK
VSHTLWDPQLVIETNGGIPPLTYQMFLHTVQIIGLPPRPTADARLEDATFVELDPEFCRS
LKLFEQLPTPEHFNVYGDNMGFLAKINWRGGETQALLLLDERLKVEQHAFERGFYLPNQA
LPNIHDSPKSMSAHLRFGCLSVRRFYWSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWR
EYFYTMSVNNPNYDRMEGNDICLSIPWAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGW
LHHTLRNTVATFLTRGGLWQSWEHGLQHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSS
LVTCPVALAKRLDPDGTYIKQYVPELMNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERI
IDLSMAVKRNMLAMKSLRNSLITPPPHCRPSNEEEVRQFFWLADLPGTGGGGC

Ligands and cofactors

IDNameFormulaCopies
FADFlavin-adenine dinucleotideC27 H33 N9 O15 P22
MGMagnesium ionMg3

Primary citation

Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome. Chandrasekaran, S., Schneps, C.M., Dunleavy, R. et al. Commun Biol (2021) 4:249-249. DOI 10.1038/s42003-021-01766-2 · PubMed

Other PDB entries of the same protein (UniProt O77059 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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