4I6E: A vertebrate cryptochrome

A vertebrate cryptochrome. Determined by X-ray diffraction at 2.7 Å resolution. Released 13 Mar 2013.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Mus musculus
Chains: 1
Atoms: 3,822
Mol. weight: 58.69 kDa
Released: 13 Mar 2013

Explore 4I6E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I6E contains 31 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: 31 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	22-26	5	1
α-helix	37-40	4
β-strand	48-55	8	1
α-helix	57-60	4
α-helix	67-85	19
β-strand	91-95	5	1
α-helix	102-109	8
β-strand	113-117	5	1
α-helix	122-137	16
β-strand	141-145	5	1
α-helix	153-159	7
α-helix	168-176	9
α-helix	179-189	11
α-helix	209-212	4
α-helix	232-242	11
α-helix	259-262	4
α-helix	270-275	6
α-helix	280-291	12
α-helix	292-294	3
α-helix	302-305	4
α-helix	306-318	13
α-helix	338-340	3
α-helix	342-350	9
α-helix	356-368	13
α-helix	373-381	9
α-helix	382-386	5
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	465-467	3
α-helix	470-476	7
β-strand	480	1	2
β-strand	484	1	2
α-helix	485-487	3
α-helix	491-506	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cryptochrome-2	A	protein	512	Mus musculus	Q9R194 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4I6E_1 Cryptochrome-2 (chains A)
MAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFA
ASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDS
EPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRMEL
PKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALARLD
KHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTP
PLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDA
IMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSC
SAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKCII
GVDYPRPIVNHAETSRLNIERMKQIYQQLSRY

Primary citation

SCFFBXL3 ubiquitin ligase targets cryptochromes at their cofactor pocket. Xing, W., Busino, L., Hinds, T.R. et al. Nature (2013) 496:64-68. DOI 10.1038/nature11964 · 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
4I6J 2.7 Å, A ubiquitin ligase-substrate complex
4U8H 2.8 Å, Crystal Structure of Mammalian Period-Cryptochrome Complex
7D0N 2.8 Å, Crystal structure of mouse CRY2 apo form

Browse structure collections

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