1L7C: Alpha-catenin fragment, residues 385-651

alpha-catenin fragment, residues 385-651. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Jun 2002.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Mus musculus
Chains: 3
Atoms: 5,544
Mol. weight: 90.62 kDa
Released: 19 Jun 2002

Explore 1L7C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L7C contains 33 α-helices and 0 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	392-396	5
α-helix	399-409	11
α-helix	413-440	28
α-helix	444-473	30
α-helix	478-506	29
α-helix	508-531	24
α-helix	535-560	26
α-helix	564-565	2
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-598	15
α-helix	608-629	22

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	399-409	11
α-helix	413-440	28
α-helix	444-471	28
α-helix	478-504	27
α-helix	508-532	25
α-helix	535-560	26
α-helix	568-577	10
α-helix	578-583	6
α-helix	585-596	12
α-helix	609-630	22

Chain C: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	399-408	10
α-helix	413-418	6
α-helix	420-439	20
α-helix	444-471	28
α-helix	484-503	20
α-helix	508-530	23
α-helix	537-560	24
α-helix	567-577	11
α-helix	578-583	6
α-helix	584-599	16
α-helix	608-629	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha E-catenin	A, B, C	protein	269	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>1L7C_1 Alpha E-catenin (chains A, B, C)
GSAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISN
NEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAV
DDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDN
YEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGI
RDIRKAVLMIRTPEELDDSDFETEDFDVR

Primary citation

Biochemical and structural definition of the l-afadin- and actin-binding sites of alpha-catenin. Pokutta, S., Drees, F., Takai, Y. et al. J Biol Chem (2002) 277:18868-18874. DOI 10.1074/jbc.M201463200 · 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
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
6O3E 4.0 Å, mouse aE-catenin 82-883
4K1N 6.5 Å, Crystal structure of full-length mouse alphaE-catenin

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