1JPW: Human Tcf-4 / beta-Catenin Complex

Crystal Structure of a Human Tcf-4 / beta-Catenin Complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 5 Dec 2001.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 6
Atoms: 12,767
Mol. weight: 192.51 kDa
Released: 5 Dec 2001

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

Secondary structure: helices and β-sheets

1JPW contains 120 α-helices and 4 β-strands across 6 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	152-160	9
α-helix	165-178	14
α-helix	182-189	8
α-helix	192-204	13
α-helix	210-221	12
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	362-366	5
α-helix	367-369	3
α-helix	375-389	15
α-helix	399-409	11
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	532-546	15
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	608-622	15
α-helix	625-632	8
α-helix	637-643	7
α-helix	649-661	13

Chain B: 37 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	153-160	8
α-helix	165-178	14
α-helix	182-189	8
α-helix	192-204	13
α-helix	208-222	15
α-helix	225-233	9
α-helix	236-242	7
α-helix	243-245	3
α-helix	249-264	16
α-helix	269-275	7
α-helix	278-284	7
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	362-366	5
α-helix	375-389	15
α-helix	399-407	9
α-helix	408-410	3
α-helix	414-426	13
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	532-546	15
β-strand	561	1	2
β-strand	564	1	2
α-helix	566-580	15
α-helix	584-591	8
α-helix	596-602	7
α-helix	608-621	14
α-helix	625-632	8
α-helix	637-643	7
α-helix	649-660	12

Chain C: 39 helices, 0 β-strands

Element	Residues	Length
α-helix	153-160	8
α-helix	165-178	14
α-helix	182-189	8
α-helix	192-204	13
α-helix	208-222	15
α-helix	225-232	8
α-helix	236-242	7
α-helix	243-245	3
α-helix	249-264	16
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	362-366	5
α-helix	375-389	15
α-helix	399-407	9
α-helix	408-410	3
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
α-helix	561-563	3
α-helix	566-580	15
α-helix	584-591	8
α-helix	596-602	7
α-helix	608-621	14
α-helix	626-632	7
α-helix	637-643	7
α-helix	649-660	12

Chains D, E and F: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	17-18	2
α-helix	42-49	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-catenin	A, B, C	protein	540	Homo sapiens	P35222 (AlphaFold model)
transcription factor 7-like 2	D, E, F	protein	49	Homo sapiens	Q9NQB0 (AlphaFold model)

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

>1JPW_1 BETA-CATENIN (chains A, B, C)
MGSHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMR
SPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDS
VLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQE
SKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHL
TDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCN
NYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYG
LPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRR
TSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENI
QRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDY

Sequence of entity 2 (D, E, F), FASTA

>1JPW_2 transcription factor 7-like 2 (chains D, E, F)
GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET

Primary citation

Structure of a human Tcf4-beta-catenin complex. Poy, F., Lepourcelet, M., Shivdasani, R.A. et al. Nat Struct Biol (2001) 8:1053-1057. DOI 10.1038/nsb720 · 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

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