1QZ7: Beta-catenin binding domain of Axin

Beta-catenin binding domain of Axin in complex with beta-catenin. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Nov 2003.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, Xenopus laevis
Chains: 2
Atoms: 4,148
Mol. weight: 65.97 kDa
Released: 18 Nov 2003

Explore 1QZ7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1QZ7 contains 42 α-helices and 2 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: 41 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	145-149	5
α-helix	150-159	10
α-helix	168-177	10
α-helix	182-189	8
α-helix	192-204	13
α-helix	210-221	12
α-helix	225-233	9
α-helix	236-242	7
α-helix	243-245	3
α-helix	249-265	17
α-helix	269-276	8
α-helix	278-284	7
α-helix	285-287	3
α-helix	291-305	15
α-helix	309-317	9
α-helix	320-328	9
α-helix	334-348	15
α-helix	353-360	8
α-helix	362-366	5
α-helix	367-369	3
α-helix	375-388	14
α-helix	389-391	3
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	561	1	1
β-strand	564	1	1
α-helix	566-580	15
α-helix	584-592	9
α-helix	596-601	6
α-helix	602-604	3
α-helix	608-621	14
α-helix	625-633	9
α-helix	637-643	7
α-helix	649-663	15

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	471-480	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-catenin	A	protein	533	Homo sapiens	P35222 (AlphaFold model)
Axin	B	protein	70	Xenopus laevis	Q9YGY0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1QZ7_1 Beta-catenin (chains A)
KHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSP
QMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVL
FYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESK
LIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTD
PSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNY
KNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLP
VVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTS
MGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQR
VAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSED

Sequence of entity 2 (B), FASTA

>1QZ7_2 Axin (chains B)
SHKLPSGPPMHHFNSRYSETGCVGMQIRDAHEENPESILDEHVQRVMKTPGCQSPGTGRH
SPKSRSPDGH

Primary citation

Crystal structure of a beta-catenin/Axin complex suggests a mechanism for the {beta}-catenin destruction complex. Xing, Y., Clements, W.K., Kimelman, D. et al. Genes Dev (2003) 17:2753-2764. DOI 10.1101/gad.1142603 · PubMed

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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