1JPP: Beta-catenin

The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin. Determined by X-ray diffraction at 3.1 Å resolution. Released 16 Jan 2002.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Mus musculus
Chains
4
Atoms
7,850
Mol. weight
121.35 kDa
Released
16 Jan 2002

Explore 1JPP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1JPP contains 81 α-helices and 2 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: 40 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix152-1598
α-helix165-17814
α-helix182-1898
α-helix194-20411
α-helix208-22114
α-helix225-2339
α-helix237-2426
α-helix243-2453
α-helix249-26517
α-helix269-2757
α-helix278-2847
α-helix285-2873
α-helix291-30515
α-helix309-3179
α-helix321-3288
α-helix334-34815
α-helix355-3606
α-helix362-3676
α-helix375-38814
α-helix389-3913
α-helix401-4077
α-helix414-42613
α-helix432-4409
α-helix443-45412
α-helix458-47114
α-helix478-48710
α-helix491-4966
α-helix504-51714
α-helix521-5233
α-helix524-5307
α-helix533-54513
α-helix566-58015
α-helix584-5918
α-helix596-6016
α-helix602-6043
α-helix608-62114
α-helix625-63410
α-helix637-6426
α-helix643-6453
α-helix649-66113
Chain B: 40 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix153-1608
α-helix167-17812
α-helix184-1896
α-helix194-20411
α-helix208-22114
α-helix225-2339
α-helix237-2426
α-helix243-2453
α-helix249-26517
α-helix269-2768
α-helix278-2847
α-helix291-30515
α-helix309-3179
α-helix321-3288
α-helix334-3429
α-helix344-3474
α-helix355-3606
α-helix362-3676
α-helix375-38814
α-helix389-3913
α-helix401-4088
α-helix414-42613
α-helix433-4408
α-helix443-45412
α-helix458-47114
α-helix478-48710
α-helix491-4966
α-helix504-51714
α-helix521-5233
α-helix524-5296
α-helix533-54412
β-strand56111
β-strand56411
α-helix566-58015
α-helix584-5918
α-helix596-6016
α-helix602-6043
α-helix608-62114
α-helix625-63410
α-helix637-6426
α-helix643-6453
α-helix649-66113
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix1027-10304

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Beta-cateninA, Bprotein538Mus musculusQ02248 (AlphaFold model)
Adenomatous polyposis coli proteinC, Dprotein15P25054
Sequence of entity 1 (A, B), FASTA
>1JPP_1 BETA-CATENIN (chains A, B)
HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQ
MVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLF
YAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKL
IILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYK
NKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPV
VVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSM
GGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
Sequence of entity 2 (C, D), FASTA
>1JPP_2 ADENOMATOUS POLYPOSIS COLI PROTEIN (chains C, D)
LDTPINYSLKYSDEQ

Primary citation

Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex. Eklof Spink, K., Fridman, S.G., Weis, W.I. EMBO J (2001) 20:6203-6212. DOI 10.1093/emboj/20.22.6203 · PubMed

Other PDB entries of the same protein (UniProt Q02248 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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