7D0N: Mouse CRY2 apo form

Crystal structure of mouse CRY2 apo form. Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Jun 2021.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Mus musculus
Chains
1
Atoms
3,393
Mol. weight
58.85 kDa
Released
23 Jun 2021

Explore 7D0N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7D0N contains 30 α-helices and 7 β-strands across 1 chain. 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, 7 β-strands

ElementResiduesLengthSheet
β-strand23-2641
α-helix37-426
β-strand49-5571
α-helix57-615
α-helix67-8620
β-strand91-9551
α-helix98-10912
β-strand113-11751
α-helix118-1192
α-helix122-13716
β-strand141-14551
α-helix153-1586
α-helix168-17710
α-helix179-1846
α-helix190-1956
α-helix197-2004
α-helix204-2074
α-helix232-24413
α-helix260-2623
α-helix270-2756
α-helix280-29314
α-helix306-31813
β-strand33912
α-helix342-3498
α-helix356-36813
α-helix373-3819
α-helix382-3865
β-strand39012
α-helix392-40211
α-helix408-41811
α-helix435-4406
α-helix445-4506
α-helix452-4543
α-helix459-4624
α-helix470-4767
α-helix485-4873
α-helix491-50616

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cryptochrome-2Aprotein514Mus musculusQ9R194 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7D0N_1 Cryptochrome-2 (chains A)
GTMAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPW
FAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEY
DSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRM
ELPKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALAR
LDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNS
TPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWI
DAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWL
SCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKC
IIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRY

Primary citation

Structural differences in the FAD-binding pockets and lid loops of mammalian CRY1 and CRY2 for isoform-selective regulation. Miller, S., Srivastava, A., Nagai, Y. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2026191118 · PubMed

Other PDB entries of the same protein (UniProt Q9R194 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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