3GDI: Period circadian protein homolog 2

Mammalian Clock Protein mPER2 - Crystal Structure of a PAS Domain Fragment. Determined by X-ray diffraction at 2.4 Å resolution. Released 19 May 2009.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Mus musculus
Chains
2
Atoms
4,300
Mol. weight
70.18 kDa
Released
19 May 2009

Explore 3GDI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GDI contains 21 α-helices and 34 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: 10 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand17011
β-strand190-19561
β-strand20112
β-strand202-20541
β-strand22412
α-helix225-2284
β-strand22911
α-helix234-2407
β-strand24811
β-strand268-27251
β-strand285-295111
β-strand306-31491
α-helix323-3253
α-helix326-3283
β-strand330-33563
β-strand34014
β-strand341-34443
α-helix348-3525
α-helix356-3594
β-strand36314
α-helix364-3674
β-strand36813
α-helix373-38513
β-strand391-39993
β-strand405-416123
β-strand423-434123
α-helix444-4452
α-helix455-46713
Chain B: 11 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand192-19655
β-strand201-20445
α-helix225-2273
β-strand22916
α-helix231-2333
α-helix234-2407
β-strand268-27366
β-strand284-28966
β-strand290-29455
β-strand307-31155
β-strand31416
α-helix315-3173
α-helix326-3283
β-strand330-33567
β-strand34018
β-strand341-34447
α-helix348-3525
α-helix356-3594
β-strand36318
α-helix365-3673
β-strand36817
α-helix375-38612
β-strand391-39997
β-strand405-416127
β-strand423-434127
α-helix444-4452
α-helix456-46712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Period circadian protein homolog 2A, Bprotein309Mus musculusO54943 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3GDI_1 Period circadian protein homolog 2 (chains A, B)
GPLGSSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAK
FVEFLAPHDVSVFHSYTTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRY
QPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQAV
DERAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRTRNGE
YITLDTSWSSFINPWSRKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQI
HRLLMQPVP

Primary citation

Structural and functional analyses of PAS domain interactions of the clock proteins Drosophila PERIOD and mouse PERIOD2. Hennig, S., Strauss, H.M., Vanselow, K. et al. PLoS Biol (2009) 7:e94-e94. DOI 10.1371/journal.pbio.1000094 · PubMed

Other PDB entries of the same protein (UniProt O54943 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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