9I8W: Catenin beta-1

Beta-catenin armadillo with cyclic peptide and Compound 3. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Feb 2026.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 4,105
Mol. weight: 61.09 kDa
Ligands: HHT
Released: 18 Feb 2026

Explore 9I8W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9I8W contains 38 α-helices and 6 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: 38 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	146-147	2
α-helix	148-152	5
α-helix	153-160	8
α-helix	165-179	15
α-helix	182-189	8
α-helix	192-204	13
α-helix	208-221	14
α-helix	225-233	9
α-helix	236-243	8
α-helix	249-265	17
α-helix	269-275	7
α-helix	278-284	7
α-helix	285-287	3
α-helix	291-305	15
α-helix	309-317	9
α-helix	320-330	11
α-helix	334-347	14
α-helix	353-359	7
α-helix	362-367	6
α-helix	375-389	15
α-helix	399-408	10
α-helix	414-427	14
α-helix	432-440	9
α-helix	443-454	12
α-helix	458-471	14
α-helix	478-487	10
α-helix	491-496	6
α-helix	504-517	14
α-helix	521-523	3
α-helix	524-529	6
α-helix	532-548	17
β-strand	560-561	2	1
β-strand	564-565	2	1
α-helix	566-580	15
α-helix	584-592	9
α-helix	596-602	7
α-helix	608-621	14
α-helix	625-633	9
α-helix	637-643	7
α-helix	649-663	15

Chain B: 0 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	2-4	3	2
β-strand	7-9	3	2
β-strand	12	1	3
β-strand	15	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Catenin beta-1	A	protein	538	Homo sapiens	P35222 (AlphaFold model)
Cyclic peptide	B	protein	16	synthetic construct

Sequence of entity 1 (A), FASTA

>9I8W_1 Catenin beta-1 (chains A)
HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQ
MVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLF
YAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKL
IILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYK
NKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPV
VVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSM
GGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK

Sequence of entity 2 (B), FASTA

>9I8W_2 Cyclic peptide (chains B)
LLVFXXVTRNDVPPDS

Ligands and cofactors

ID	Name	Formula	Copies
HHT	2-(4-bromanyl-2-methoxy-phenyl)ethanoic acid	C9 H9 Br O3	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Beta-catenin armadillo with cyclic peptide and Compound 3. Klejnot, M., Skowron, A.N., Pastok, M.W. et al. To be published.

Other PDB entries of the same protein (UniProt P35222 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FQN 1.65 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
3FQR 1.7 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
7AFW 1.81 Å, Beta-Catenin in complex with compound 6
1JDH 1.9 Å, Crystal structure of beta-catenin and htcf-4
9I8K 2.0 Å, Beta-catenin armadillo (150-663)
9I8X 2.0 Å, Beta-catenin armadillo with cyclic peptide and Compound 2
8RU3 2.0 Å, Crystal structure of beta-catenin in complex with alpha-helical peptide inhibitor
6M90 2.05 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-2776 ternary complex
29KL 2.09 Å, Crystal structure of Human Catenin Beta-1 in complex with cyclic beta sheet peptide…
1G3J 2.1 Å, Crystal structure of the XTCF3-cbd/beta-catenin armadillo repeat complex
1T08 2.1 Å, Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3
3DIW 2.1 Å, c-terminal beta-catenin bound TIP-1 structure

Browse structure collections

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