7DLI: Mouse CRY1

Crystal structure of mouse CRY1 in complex with KL001 compound. Determined by X-ray diffraction at 2.2 Å resolution. Released 23 Jun 2021.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 3
Atoms: 11,251
Mol. weight: 173.37 kDa
Ligands: H8X
Released: 23 Jun 2021

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

Secondary structure: helices and β-sheets

7DLI contains 95 α-helices and 30 β-strands across 3 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: 34 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	19-25	7
β-strand	30-36	7	1
α-helix	49-67	19
β-strand	73-76	4	1
α-helix	80-91	12
β-strand	95-99	5	1
α-helix	104-119	16
α-helix	122	1
β-strand	123-127	5	1
α-helix	135-141	7
α-helix	150-159	10
α-helix	161-169	9
α-helix	172-175	4
β-strand	179	1	1
α-helix	186-190	5
α-helix	191-194	4
α-helix	205-208	4
α-helix	214-230	17
α-helix	236-239	4
α-helix	241-244	4
α-helix	246-247	2
α-helix	252-257	6
α-helix	262-276	15
α-helix	281-283	3
α-helix	284-287	4
α-helix	288-300	13
β-strand	321	1	2
α-helix	324-331	8
α-helix	338-350	13
α-helix	355-363	9
α-helix	364-368	5
β-strand	372	1	2
α-helix	374-384	11
α-helix	390-400	11
α-helix	418-421	4
α-helix	427-432	6
α-helix	434-436	3
α-helix	447-449	3
α-helix	452-458	7
β-strand	462	1	3
β-strand	466	1	3
α-helix	467-469	3
α-helix	473-487	15

Chain B: 31 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	4
α-helix	19-25	7
β-strand	30-37	8	4
α-helix	49-68	20
β-strand	73-77	5	4
α-helix	80-91	12
β-strand	95-99	5	4
α-helix	104-119	16
β-strand	123-127	5	4
α-helix	135-141	7
α-helix	150-158	9
α-helix	161-170	10
α-helix	172-175	4
β-strand	179	1	4
α-helix	186-190	5
α-helix	191-194	4
α-helix	214-229	16
α-helix	239-241	3
α-helix	246-247	2
α-helix	252-257	6
α-helix	262-277	16
α-helix	284-287	4
α-helix	288-300	13
β-strand	321	1	5
α-helix	324-331	8
α-helix	338-350	13
α-helix	355-363	9
α-helix	364-368	5
β-strand	372	1	5
α-helix	374-384	11
α-helix	390-400	11
α-helix	417-422	6
α-helix	427-432	6
α-helix	434-436	3
α-helix	441-444	4
α-helix	447-449	3
α-helix	452-457	6
β-strand	462	1	6
β-strand	466	1	6
α-helix	467-469	3
α-helix	473-489	17

Chain C: 30 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	7
α-helix	19-25	7
β-strand	30-37	8	7
α-helix	49-68	20
β-strand	73-77	5	7
α-helix	80-91	12
β-strand	93-99	7	7
α-helix	104-119	16
β-strand	123-127	5	7
α-helix	135-141	7
α-helix	150-158	9
α-helix	161-170	10
α-helix	172-175	4
β-strand	179	1	7
α-helix	186-190	5
α-helix	191-194	4
α-helix	214-229	16
α-helix	252-257	6
α-helix	262-277	16
α-helix	284-287	4
α-helix	288-300	13
β-strand	321	1	8
α-helix	324-331	8
α-helix	338-350	13
α-helix	355-363	9
α-helix	364-368	5
β-strand	372	1	8
α-helix	374-384	11
α-helix	390-400	11
α-helix	409-411	3
α-helix	417-422	6
α-helix	427-432	6
α-helix	434-436	3
α-helix	441-444	4
α-helix	447-449	3
α-helix	452-458	7
β-strand	462	1	9
β-strand	466	1	9
α-helix	467-469	3
α-helix	473-495	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cryptochrome-1	A, B, C	protein	498	Mus musculus	P97784 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>7DLI_1 Cryptochrome-1 (chains A, B, C)
GTMGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQC
LEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLAT
EAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKC
MTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPR
MNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYT
AATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLAR
HAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGF
GRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASR
LNIERMKQIYQQLSRYRG

Ligands and cofactors

ID	Name	Formula	Copies
H8X	N-[(2R)-3-carbazol-9-yl-2-oxidanyl-propyl]-N-(furan-2-ylmethyl)methanesulfonami…	C21 H22 N2 O4 S	3

Water and common crystallization additives (EDO) are not listed.

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 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
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
4K0R 2.65 Å, Crystal structure of mouse Cryptochrome 1

Browse structure collections

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