6OF7: CRY1-PER2 complex

Crystal structure of the CRY1-PER2 complex. Determined by X-ray diffraction at 3.11 Å resolution. Released 4 Mar 2020.

Method: X-ray diffraction
Resolution: 3.11 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 4,424
Mol. weight: 71.2 kDa
Released: 4 Mar 2020

Explore 6OF7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6OF7 contains 31 α-helices and 9 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: 25 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	19-24	6
β-strand	30	1	1
β-strand	33-37	5	1
α-helix	50-67	18
β-strand	73-77	5	1
α-helix	80-91	12
β-strand	93-99	7	1
α-helix	104-118	15
β-strand	123-127	5	1
α-helix	135-142	8
α-helix	150-157	8
α-helix	161-170	10
α-helix	172-175	4
β-strand	179	1	1
α-helix	196-198	3
α-helix	214-226	13
α-helix	246-247	2
α-helix	252-257	6
α-helix	262-276	15
α-helix	288-300	13
α-helix	324-332	9
α-helix	338-350	13
α-helix	355-365	11
α-helix	374-384	11
α-helix	390-400	11
α-helix	411-414	4
α-helix	427-432	6
α-helix	434-436	3
α-helix	447-449	3
α-helix	452-456	5
β-strand	462	1	2
β-strand	466	1	2
α-helix	473-490	18

Chain B: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	1134-1137	4
α-helix	1138-1142	5
α-helix	1155-1157	3
α-helix	1160-1173	14
α-helix	1183-1190	8
α-helix	1194-1198	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cryptochrome-1	A	protein	491	Mus musculus	P97784 (AlphaFold model)
Period circadian protein homolog 2	B	protein	128	Homo sapiens	O15055 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6OF7_1 Cryptochrome-1 (chains A)
MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLE
DLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEA
GVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKCMT
PLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMN
ANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAA
TNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHA
VACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGR
RTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLN
IERMKQIYQQL

Sequence of entity 2 (B), FASTA

>6OF7_2 Period circadian protein homolog 2 (chains B)
GAMDPEFSSDTSHTSKYFGSIDSSENNHKAKMNTGMEESEHFIKCVLQDPIWLLMADADS
SVMMTYQLPSRNLEAVLKEDREKLKLLQKLQPRFTESQKQELREVHQWMQTGGLPAAIDV
AECVYCES

Primary citation

Dynamics at the serine loop underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing. Fribourgh, J.L., Srivastava, A., Sandate, C.R. et al. Elife (2020) 9. DOI 10.7554/eLife.55275 · PubMed

Other PDB entries of the same protein (UniProt P97784 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5T5X 1.84 Å, High resolution structure of mouse Cryptochrome 1
7D1C 1.91 Å, Crystal structure of mouse Cryptochrome 1 in complex with compound TH303
7D0M 1.95 Å, Crystal structure of mouse CRY1 with bound cryoprotectant
6KX4 2.0 Å, Crystal structure of mouse Cryptochrome 1 apo form
6KX5 2.0 Å, Crystal structure of mouse Cryptochrome 1 in complex with KL044 compound
6KX6 2.0 Å, Crystal structure of mouse Cryptochrome 1 in complex with KL101 compound
7WVA 2.05 Å, Crystal structure of mouse Cryptochrome 1 in complex with TH401 compound
6KX7 2.1 Å, Crystal structure of mouse Cryptochrome 1 in complex with TH301 compound
6LUE 2.1 Å, Crystal structure of mouse Cryptochrome 1 in complex with compound KL201
7DLI 2.2 Å, Crystal structure of mouse CRY1 in complex with KL001 compound
7D19 2.35 Å, Crystal structure of mouse Cryptochrome 1 in complex with compound TH129
4CT0 2.45 Å, Crystal Structure of Mouse Cryptochrome1 in Complex with Period2

Browse structure collections

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