4K03: Drosophila Cryprochrome

Crystal structure of Drosophila Cryprochrome. Determined by X-ray diffraction at 3.2 Å resolution. Released 26 Jun 2013.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Drosophila melanogaster
Chains
2
Atoms
8,746
Mol. weight
130.29 kDa
Ligands
FAD
Released
26 Jun 2013

Explore 4K03 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K03 contains 64 α-helices and 26 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: 30 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand6-1161
α-helix21-255
α-helix341
β-strand35-4281
α-helix54-7219
β-strand82-8541
α-helix88-9811
β-strand103-10751
α-helix114-12815
β-strand131-13551
α-helix143-1497
β-strand15712
α-helix158-16710
α-helix177-1793
β-strand18511
α-helix190-1967
α-helix205-2084
α-helix226-24621
α-helix267-2715
α-helix277-28812
β-strand29613
β-strand30113
α-helix303-3053
α-helix306-32116
α-helix347-3559
α-helix361-37313
α-helix378-38811
α-helix398-40710
α-helix413-42513
α-helix430-4334
α-helix435-4384
α-helix444-4474
α-helix452-4576
α-helix459-4613
α-helix472-4743
α-helix477-4826
β-strand48714
β-strand49114
α-helix498-51417
α-helix519-5202
β-strand52412
α-helix528-5358
Chain B: 34 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix-1-46
β-strand6-1165
β-strand1816
α-helix21-277
α-helix341
β-strand35-4285
α-helix54-7421
β-strand82-8545
α-helix88-9811
β-strand103-10755
α-helix112-1143
α-helix115-12814
β-strand131-13555
α-helix143-1497
α-helix154-1552
α-helix158-16710
α-helix171-1766
β-strand17716
α-helix1781
α-helix190-1956
β-strand19815
α-helix205-2084
α-helix227-24620
α-helix267-2715
α-helix277-28812
β-strand29617
β-strand30117
α-helix303-3053
α-helix306-32015
α-helix347-3537
α-helix361-37313
α-helix378-38811
β-strand38918
β-strand39418
α-helix397-40711
α-helix413-42412
α-helix430-4334
α-helix435-4384
α-helix441-4477
α-helix452-4576
α-helix459-4613
α-helix472-4743
α-helix477-4826
β-strand48819
β-strand49119
α-helix498-51417
α-helix519-5202
α-helix528-5347

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cryptochrome-1A, Bprotein561Drosophila melanogasterO77059 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4K03_1 Cryptochrome-1 (chains A, B)
GAMGSGIQRPTSTSSLVAAMATRGANVIWFRHGLRLHDNPALLAALADKDQGIALIPVFI
FDGESAGTKNVGYNRMRFLLDSLQDIDDQLQAATDGRGRLLVFEGEPAYIFRRLHEQVRL
HRICIEQDCEPIWNERDESIRSLCRELNIDFVEKVSHTLWDPQLVIETNGGIPPLTYQMF
LHTVQIIGLPPRPTADARLEDATFVELDPEFCRSLKLFEQLPTPEHFNVYGDNMGFLAKI
NWRGGETQALLLLDERLKVEQHAFERGFYLPNQALPNIHDSPKSMSAHLRFGCLSVRRFY
WSVHDLFKNVQLRACVRGVQMTGGAHITGQLIWREYFYTMSVNNPNYDRMEGNDICLSIP
WAKPNENLLQSWRLGQTGFPLIDGAMRQLLAEGWLHHTLRNTVATFLTRGGLWQSWEHGL
QHFLKYLLDADWSVCAGNWMWVSSSAFERLLDSSLVTCPVALAKRLDPDGTYIKQYVPEL
MNVPKEFVHEPWRMSAEQQEQYECLIGVHYPERIIDLSMAVKRNMLAMKSLRNSLITPPP
HCRPSNEEEVRQFFWLADVVV

Ligands and cofactors

IDNameFormulaCopies
FADFlavin-adenine dinucleotideC27 H33 N9 O15 P22

Primary citation

Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function. Czarna, A., Berndt, A., Singh, H.R. et al. Cell (2013) 153:1394-1405. DOI 10.1016/j.cell.2013.05.011 · PubMed

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

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