4IGG: Catenin alpha-1

Full-length human alpha-catenin crystal structure. Determined by X-ray diffraction at 3.66 Å resolution. Released 26 Dec 2012.

Method
X-ray diffraction
Resolution
3.66 Å
Organism
Homo sapiens
Chains
2
Atoms
11,714
Mol. weight
184.61 kDa
Ligands
PO4
Released
26 Dec 2012

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

Secondary structure: helices and β-sheets

4IGG contains 54 α-helices and 7 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: 27 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix84-11330
α-helix118-16548
α-helix170-19728
α-helix201-23030
α-helix235-25925
α-helix277-29014
α-helix301-32020
α-helix327-35226
α-helix361-39333
α-helix399-40911
α-helix413-43927
α-helix444-47330
α-helix478-50427
α-helix508-53124
α-helix535-55925
α-helix567-57711
α-helix578-5836
α-helix584-59815
α-helix608-63023
α-helix669-6746
α-helix678-70225
α-helix711-72919
α-helix739-76224
α-helix771-79525
β-strand809-81021
α-helix811-83424
α-helix838-84710
α-helix858-8603
Chain B: 27 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix86-11328
α-helix118-16548
α-helix170-19728
α-helix201-23030
α-helix235-25925
β-strand261-26221
α-helix277-28812
α-helix305-32016
α-helix327-35327
α-helix362-39332
α-helix399-40911
α-helix413-43927
α-helix444-47330
α-helix478-50427
α-helix508-53124
α-helix535-56026
α-helix567-57711
α-helix578-5836
α-helix584-59916
α-helix608-62922
β-strand63112
α-helix669-6746
α-helix678-70225
β-strand705-70623
α-helix712-72918
α-helix739-76628
α-helix770-79324
β-strand80112
β-strand80812
α-helix813-84129
β-strand860-86123
α-helix862-8632
α-helix866-87712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Catenin alpha-1A, Bprotein832Homo sapiensP35221 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4IGG_1 Catenin alpha-1 (chains A, B)
ESQFLKEELVAAVEDVRKQGDLMKAAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLIL
ADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDV
GHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQA
TASDDASQHQGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMAD
SSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQ
LRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSIS
NNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDA
VDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMD
NYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDG
IRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQK
AKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSD
VISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQ
NLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKM
KAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSIPHHHHHH

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P2

Primary citation

Dimer asymmetry defines alpha-catenin interactions. Rangarajan, E.S., Izard, T. Nat Struct Mol Biol (2013) 20:188-193. DOI 10.1038/nsmb.2479 · PubMed

Other PDB entries of the same protein (UniProt P35221 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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