4MLP: Mammalian cryptochrome

Mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase. Determined by X-ray diffraction at 1.94 Å resolution. Released 16 Oct 2013.

Method
X-ray diffraction
Resolution
1.94 Å
Organism
Mus musculus
Chains
4
Atoms
17,726
Mol. weight
236.35 kDa
Ligands
2CX
Released
16 Oct 2013

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

Secondary structure: helices and β-sheets

4MLP contains 149 α-helices and 37 β-strands across 4 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: 37 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand22-2654
α-helix37-437
β-strand48-5584
α-helix59-613
α-helix67-8620
β-strand91-9554
α-helix98-10912
β-strand113-11754
α-helix122-13716
β-strand141-14554
α-helix153-1597
α-helix168-1769
α-helix179-18911
α-helix190-1934
α-helix197-2015
α-helix204-2085
α-helix210-2123
α-helix213-2164
α-helix232-24211
α-helix245-2484
α-helix249-2535
α-helix259-2624
α-helix264-2652
α-helix270-2756
α-helix280-29415
α-helix299-3013
α-helix302-3054
α-helix306-31914
β-strand33915
α-helix342-3498
α-helix356-36813
α-helix373-3819
α-helix382-3865
β-strand39015
α-helix392-40211
α-helix408-41811
α-helix429-4324
α-helix435-4406
α-helix445-4506
α-helix452-4543
α-helix465-4673
α-helix470-4767
β-strand48016
β-strand48416
α-helix485-4873
α-helix491-50717
Chain B: 37 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand22-2767
α-helix37-437
β-strand48-5587
α-helix59-613
α-helix67-8519
β-strand91-9557
α-helix98-10912
β-strand113-11757
α-helix122-13716
β-strand141-14557
α-helix153-1597
α-helix168-1769
α-helix179-18911
α-helix190-1956
α-helix197-2015
α-helix204-2085
α-helix210-2123
α-helix213-2164
α-helix232-24211
α-helix245-2484
α-helix249-2535
α-helix259-2624
α-helix264-2652
α-helix270-2756
α-helix280-29415
α-helix299-3013
α-helix302-3054
α-helix306-31813
β-strand33918
α-helix342-3509
α-helix356-36813
α-helix373-3819
α-helix382-3865
β-strand39018
α-helix392-40211
α-helix408-41811
α-helix429-4324
α-helix435-4406
α-helix445-4506
α-helix452-4543
α-helix465-4673
α-helix470-4767
β-strand48019
β-strand48419
α-helix485-4873
α-helix491-50717
Chain C: 37 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand22-2651
α-helix37-437
β-strand48-5581
α-helix59-613
α-helix67-8519
β-strand91-9551
α-helix98-10912
β-strand113-11751
α-helix122-13716
β-strand141-14551
α-helix153-1597
α-helix168-1769
α-helix179-18911
α-helix190-1945
α-helix197-2015
α-helix204-2085
α-helix209-2124
α-helix232-24211
α-helix245-2484
α-helix249-2535
α-helix259-2624
α-helix264-2652
α-helix270-2756
α-helix280-29415
α-helix299-3013
α-helix302-3054
α-helix306-31813
β-strand33912
α-helix342-3509
α-helix356-36813
α-helix373-3819
α-helix382-3865
β-strand39012
α-helix392-40211
α-helix408-41811
α-helix429-4324
α-helix435-4406
α-helix445-4506
α-helix452-4543
α-helix459-4624
α-helix465-4673
α-helix470-4756
β-strand48013
β-strand48413
α-helix485-4873
α-helix491-50717
Chain D: 38 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand22-27610
α-helix37-437
β-strand48-55810
α-helix59-613
α-helix67-8519
β-strand91-95510
α-helix98-10912
β-strand113-117510
α-helix122-13716
β-strand141-145510
α-helix153-1597
α-helix168-1769
α-helix179-18911
α-helix190-1956
β-strand197110
α-helix198-1992
α-helix204-2085
α-helix209-2124
α-helix213-2164
α-helix232-24211
α-helix245-2484
α-helix249-2535
α-helix259-2624
α-helix264-2652
α-helix270-2756
α-helix280-29516
α-helix299-3013
α-helix302-3054
α-helix306-31813
β-strand339111
α-helix342-3509
α-helix356-36813
α-helix373-3819
α-helix382-3865
β-strand390111
α-helix392-40211
α-helix408-41811
α-helix430-4323
α-helix435-4406
α-helix445-4506
α-helix452-4543
α-helix459-4624
α-helix465-4673
α-helix470-4767
β-strand480112
β-strand484112
α-helix485-4873
α-helix491-50717

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cryptochrome-2A, B, C, Dprotein512Mus musculusQ9R194 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4MLP_1 Cryptochrome-2 (chains A, B, C, D)
MAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFA
ASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDS
EPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRMEL
PKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALARLD
KHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTP
PLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDA
IMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSC
SAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKCII
GVDYPRPIVNHAETSRLNIERMKQIYQQLSRY

Ligands and cofactors

IDNameFormulaCopies
2CXN-[(2S)-3-(9H-carbazol-9-yl)-2-hydroxypropyl]-N-(furan-2-ylmethyl)methanesulfon…C21 H22 N2 O4 S4

Primary citation

Crystal structure of mammalian cryptochrome in complex with a small molecule competitor of its ubiquitin ligase. Nangle, S., Xing, W., Zheng, N. Cell Res (2013) 23:1417-1419. DOI 10.1038/cr.2013.136 · PubMed

Other PDB entries of the same protein (UniProt Q9R194 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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