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

Element	Residues	Length	Sheet
α-helix	84-113	30
α-helix	118-165	48
α-helix	170-197	28
α-helix	201-230	30
α-helix	235-259	25
α-helix	277-290	14
α-helix	301-320	20
α-helix	327-352	26
α-helix	361-393	33
α-helix	399-409	11
α-helix	413-439	27
α-helix	444-473	30
α-helix	478-504	27
α-helix	508-531	24
α-helix	535-559	25
α-helix	567-577	11
α-helix	578-583	6
α-helix	584-598	15
α-helix	608-630	23
α-helix	669-674	6
α-helix	678-702	25
α-helix	711-729	19
α-helix	739-762	24
α-helix	771-795	25
β-strand	809-810	2	1
α-helix	811-834	24
α-helix	838-847	10
α-helix	858-860	3

Chain B: 27 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	86-113	28
α-helix	118-165	48
α-helix	170-197	28
α-helix	201-230	30
α-helix	235-259	25
β-strand	261-262	2	1
α-helix	277-288	12
α-helix	305-320	16
α-helix	327-353	27
α-helix	362-393	32
α-helix	399-409	11
α-helix	413-439	27
α-helix	444-473	30
α-helix	478-504	27
α-helix	508-531	24
α-helix	535-560	26
α-helix	567-577	11
α-helix	578-583	6
α-helix	584-599	16
α-helix	608-629	22
β-strand	631	1	2
α-helix	669-674	6
α-helix	678-702	25
β-strand	705-706	2	3
α-helix	712-729	18
α-helix	739-766	28
α-helix	770-793	24
β-strand	801	1	2
β-strand	808	1	2
α-helix	813-841	29
β-strand	860-861	2	3
α-helix	862-863	2
α-helix	866-877	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catenin alpha-1	A, B	protein	832	Homo sapiens	P35221 (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

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

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:

6V2O 1.27 Å, HLA-B*57:01 presenting the peptide ASLNLPAVSW
6V2P 1.3 Å, HLA-B*57:03 presenting the peptide ASLNLPAVSW
9BL4 1.75 Å, KIR3DL1*086 in complex with HLA-B*57:03 presenting the AW10 peptide
9BL3 2.0 Å, KIR3DL1*114 in complex with HLA-B*57:03 presenting the AW10 peptide
9BL2 2.1 Å, KIR3DL1*001 in complex with HLA-B*57:03 presenting the AW10 peptide
1H6G 2.2 Å, alpha-catenin M-domain
4EHP 2.66 Å, Crystal Structure of human vinculin head domain (residues 1-252) in complex with…
7UTJ 2.77 Å, Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin
6UPV 3.2 Å, Alpha-E-catenin ABD-F-actin complex

Browse structure collections

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