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

Element	Residues	Length	Sheet
β-strand	23-26	4	1
α-helix	37-42	6
β-strand	49-55	7	1
α-helix	57-61	5
α-helix	67-86	20
β-strand	91-95	5	1
α-helix	98-109	12
β-strand	113-117	5	1
α-helix	118-119	2
α-helix	122-137	16
β-strand	141-145	5	1
α-helix	153-158	6
α-helix	168-177	10
α-helix	179-184	6
α-helix	190-195	6
α-helix	197-200	4
α-helix	204-207	4
α-helix	232-244	13
α-helix	260-262	3
α-helix	270-275	6
α-helix	280-293	14
α-helix	306-318	13
β-strand	339	1	2
α-helix	342-349	8
α-helix	356-368	13
α-helix	373-381	9
α-helix	382-386	5
β-strand	390	1	2
α-helix	392-402	11
α-helix	408-418	11
α-helix	435-440	6
α-helix	445-450	6
α-helix	452-454	3
α-helix	459-462	4
α-helix	470-476	7
α-helix	485-487	3
α-helix	491-506	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cryptochrome-2	A	protein	514	Mus musculus	Q9R194 (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:

7V8Y 1.9 Å, Crystal structure of mouse CRY2 in complex with SHP1703 compound
4MLP 1.94 Å, Mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase
7V8Z 1.95 Å, Crystal structure of mouse CRY2 in complex with SHP656 compound
4I6G 2.2 Å, a vertebrate cryptochrome with FAD
6KX8 2.25 Å, Crystal structure of mouse Cryptochrome 2 in complex with TH301 compound
7EJ9 2.6 Å, Alternative crystal structure of mouse Cryptochrome 2 in complex with TH301 compound
4I6E 2.7 Å, A vertebrate cryptochrome
4I6J 2.7 Å, A ubiquitin ligase-substrate complex
4U8H 2.8 Å, Crystal Structure of Mammalian Period-Cryptochrome Complex

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