6O3E: Mouse aE-catenin 82-883

mouse aE-catenin 82-883. Determined by X-ray diffraction at 4.0 Å resolution. Released 13 Nov 2019.

Method: X-ray diffraction
Resolution: 4.0 Å
Organism: Mus musculus
Chains: 2
Atoms: 8,070
Mol. weight: 178.14 kDa
Released: 13 Nov 2019

Explore 6O3E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6O3E contains 41 α-helices and 0 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: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	87-113	27
α-helix	118-166	49
α-helix	170-196	27
α-helix	202-228	27
α-helix	235-260	26
α-helix	277-287	11
α-helix	302-320	19
α-helix	327-350	24
α-helix	351-353	3
α-helix	365-391	27
α-helix	399-409	11
α-helix	413-439	27
α-helix	444-473	30
α-helix	478-503	26
α-helix	508-531	24
α-helix	535-560	26
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-598	15
α-helix	608-629	22

Chain B: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	84-111	28
α-helix	120-165	46
α-helix	172-176	5
α-helix	181-197	17
α-helix	201-230	30
α-helix	235-260	26
α-helix	277-287	11
α-helix	303-304	2
α-helix	305-319	15
α-helix	327-352	26
α-helix	363-393	31
α-helix	399-408	10
α-helix	414-439	26
α-helix	444-473	30
α-helix	478-504	27
α-helix	508-531	24
α-helix	535-560	26
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-598	15
α-helix	608-629	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catenin alpha-1	A, B	protein	806	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6O3E_1 Catenin alpha-1 (chains A, B)
GGILESQFLKEELVVAVEDVRKQGDLMKSAAGEFADDPSSSVKRGNMVRAARALLSAVTR
LLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQE
LKDVGNRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISN
AAQATASDDAAQHQGGSGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAA
LMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRD
LRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLA
CSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRV
LTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVT
SEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRL
VYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLP
QEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLK
NTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVK
AEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAV
SWKMKAPEKKPLVKREKQDETQTKIK

Primary citation

Binding partner- and force-promoted changes in alpha E-catenin conformation probed by native cysteine labeling. Terekhova, K., Pokutta, S., Kee, Y.S. et al. Sci Rep (2019) 9:15375-15375. DOI 10.1038/s41598-019-51816-3 · PubMed

Other PDB entries of the same protein (UniProt P26231 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DOW 1.8 Å, Crystal structure of a chimera of beta-catenin and alpha-catenin
6DV1 2.2 Å, Crystal structure of the alpha-E-catenin actin-binding domain
4E17 2.3 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
4E18 2.4 Å, Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
1L7C 2.5 Å, alpha-catenin fragment, residues 385-651
5Y04 2.85 Å, Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin
1DOV 3.0 Å, Crystal structure of the alpha-catenin dimerization domain
9DVA 3.1 Å, F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin
6WVT 3.56 Å, Structural basis of alphaE-catenin - F-actin catch bond behavior
4K1N 6.5 Å, Crystal structure of full-length mouse alphaE-catenin

Browse structure collections

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