3IFQ: Plakoglobin

Interction of plakoglobin and beta-catenin with desmosomal cadherins. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Sept 2009.

Method
X-ray diffraction
Resolution
2.8 Å
Organisms
Homo sapiens, Mus musculus
Chains
4
Atoms
9,726
Mol. weight
145.55 kDa
Released
15 Sept 2009

Explore 3IFQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IFQ contains 99 α-helices and 4 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: 42 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix127-1315
α-helix133-14210
α-helix144-1518
α-helix156-16914
α-helix173-1808
α-helix183-19311
α-helix199-21214
α-helix216-2249
α-helix227-2337
α-helix234-2363
α-helix240-25617
α-helix260-2667
α-helix269-2724
α-helix274-2785
α-helix282-29615
α-helix300-3089
α-helix311-32111
α-helix325-33814
α-helix344-3507
α-helix353-3586
α-helix359-3624
α-helix366-38015
α-helix390-3978
α-helix405-41814
α-helix423-4297
α-helix434-44512
α-helix449-46214
α-helix469-4779
α-helix481-4877
α-helix488-4903
α-helix495-50814
α-helix512-5143
α-helix515-5206
α-helix523-54321
α-helix556-57015
α-helix574-5829
α-helix586-5927
α-helix598-61114
α-helix615-6239
α-helix627-6337
α-helix639-65113
α-helix662-6676
Chain B: 41 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix127-1315
α-helix133-1419
α-helix144-1529
α-helix156-16914
α-helix173-1819
α-helix183-19311
α-helix199-21214
α-helix216-2249
α-helix227-2337
α-helix240-25516
α-helix261-2666
α-helix269-2735
α-helix274-2763
α-helix282-29615
α-helix300-3089
α-helix311-32111
α-helix325-33814
α-helix344-3507
α-helix353-3586
α-helix359-3624
α-helix366-37914
α-helix390-3989
α-helix405-41814
α-helix423-4308
α-helix434-44512
α-helix452-46211
α-helix469-47810
α-helix481-4877
α-helix488-4903
α-helix495-51016
α-helix512-5143
α-helix515-5206
α-helix523-54018
α-helix556-57015
α-helix574-5829
α-helix586-5927
α-helix598-61114
α-helix615-6239
α-helix627-6337
α-helix639-65113
α-helix663-6697
Chain C: 8 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand629-63351
α-helix639-6413
α-helix643-6464
α-helix653-66412
α-helix6721
β-strand674-67851
α-helix691-6933
α-helix706-7105
α-helix713-7153
α-helix716-7194
Chain D: 8 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand629-63352
α-helix634-6352
α-helix640-6478
α-helix650-6523
α-helix653-66412
α-helix672-6732
β-strand674-67852
α-helix691-6933
α-helix706-7105
α-helix716-7205

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
plakoglobinA, Bprotein553Homo sapiensP14923 (AlphaFold model)
E-cadherinC, Dprotein107Mus musculusP09803 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3IFQ_1 plakoglobin (chains A, B)
KSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSP
QLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVL
FYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESK
LIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTS
NSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNS
KNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIP
AIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVA
AGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRV
AAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKR
VSVELTNSLFKHD
Sequence of entity 2 (C, D), FASTA
>3IFQ_2 E-cadherin (chains C, D)
LDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDY
EGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD

Primary citation

Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. Choi, H.J., Gross, J.C., Pokutta, S. et al. J Biol Chem (2009) 284:31776-31788. DOI 10.1074/jbc.M109.047928 · PubMed

Other PDB entries of the same protein (UniProt P14923 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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