4K1N: Full-length mouse alphaE-catenin

Crystal structure of full-length mouse alphaE-catenin. Determined by X-ray diffraction at 6.5 Å resolution. Released 1 May 2013.

Method: X-ray diffraction
Resolution: 6.5 Å
Organism: Mus musculus
Chains: 2
Atoms: 8,020
Mol. weight: 201.62 kDa
Released: 1 May 2013

Explore 4K1N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K1N contains 45 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: 22 helices, 0 β-strands

Element	Residues	Length
α-helix	86-112	27
α-helix	118-165	48
α-helix	170-197	28
α-helix	201-230	30
α-helix	235-258	24
α-helix	293-297	5
α-helix	306-312	7
α-helix	327-350	24
α-helix	365-369	5
α-helix	377-386	10
α-helix	387-391	5
α-helix	404-408	5
α-helix	414-439	26
α-helix	444-472	29
α-helix	478-505	28
α-helix	508-531	24
α-helix	535-560	26
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-595	12
α-helix	604-606	3
α-helix	608-630	23

Chain B: 23 helices, 0 β-strands

Element	Residues	Length
α-helix	86-112	27
α-helix	118-165	48
α-helix	170-197	28
α-helix	201-230	30
α-helix	235-258	24
α-helix	293-297	5
α-helix	306-312	7
α-helix	327-350	24
α-helix	365-369	5
α-helix	375-377	3
α-helix	378-386	9
α-helix	387-391	5
α-helix	404-408	5
α-helix	414-439	26
α-helix	444-472	29
α-helix	478-505	28
α-helix	508-531	24
α-helix	535-560	26
α-helix	567-578	12
α-helix	579-583	5
α-helix	584-595	12
α-helix	604-606	3
α-helix	608-630	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catenin alpha-1	A, B	protein	912	Mus musculus	P26231 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4K1N_1 Catenin alpha-1 (chains A, B)
GSHMASMTAVHAGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGR
SKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVVAVEDVRKQGDLMKSAAGEFADD
PCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLG
IQYKALKPEVDKLNIMAAKRQQELKDVGNRDQMAAARGILQKNVPILYTASQACLQHPDV
AAYKANRDLIYKQLQQAVTGISNAAQATASDDAAQHQGGSGGELAYALNNFDKQIIVDPL
SFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGN
AGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEK
EVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAK
PQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKD
VDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAA
VEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRT
SVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIV
LAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQ
DLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVK
ASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPV
QALSEFKAMDSI

Primary citation

An autoinhibited structure of alpha-catenin and its implications for vinculin recruitment to adherens junctions. Ishiyama, N., Tanaka, N., Abe, K. et al. J Biol Chem (2013) 288:15913-15925. DOI 10.1074/jbc.M113.453928 · 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
6O3E 4.0 Å, mouse aE-catenin 82-883

Browse structure collections

About this viewer

MolViewer shows 4K1N directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.