4CDJ: ZNRF3 ectodomain

Structure of ZNRF3 ectodomain. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 Jan 2014.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: MUS MUSCULUS
Chains: 2
Atoms: 2,750
Mol. weight: 36.33 kDa
Released: 8 Jan 2014

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

Secondary structure: helices and β-sheets

4CDJ contains 15 α-helices and 14 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: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	58-67	10	1
α-helix	73-74	2
β-strand	75-85	11	1
β-strand	94-100	7	1
α-helix	103-106	4
α-helix	113-115	3
β-strand	120-125	6	1
α-helix	126-128	3
α-helix	129-131	3
α-helix	139-148	10
β-strand	151-157	7	1
α-helix	164-168	5
β-strand	180-183	4	1
α-helix	185-195	11
β-strand	201-207	7	1

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	58-68	11	2
β-strand	74-85	12	2
β-strand	94-100	7	2
α-helix	103-106	4
α-helix	113-115	3
β-strand	120-125	6	2
α-helix	126-128	3
α-helix	129-131	3
α-helix	139-148	10
β-strand	151-157	7	2
α-helix	164-168	5
β-strand	180-183	4	2
α-helix	185-195	11
β-strand	201-206	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase ZNRF3	A, B	protein	164	MUS MUSCULUS	Q5SSZ7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4CDJ_1 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 (chains A, B)
GSKETAFVEVVLFESSPSGDYTTHTTGLTGRFSRAGAMLSAEGEIVQMHPLGLCNNNDEE
DLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGSE
DPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHLAAAHHHHHH

Primary citation

Structures of Wnt-Antagonist Znrf3 and its Complex with R-Spondin 1 and Implications for Signaling. Peng, W.C., De Lau, W., Madoori, P.K. et al. PLoS One (2013) 8:83110. DOI 10.1371/JOURNAL.PONE.0083110 · PubMed

Other PDB entries of the same protein (UniProt Q5SSZ7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4C86 2.0 Å, mouse ZNRF3 ectodomain crystal form I
4C8P 2.1 Å, mouse ZNRF3 ectodomain crystal form V, disulfide-bridged S90C variant
4C8C 2.4 Å, mouse ZNRF3 ectodomain crystal form III
4C9A 2.4 Å, Mouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form I
4C8F 2.69 Å, mouse ZNRF3 ectodomain crystal form IV
4C8A 2.7 Å, mouse ZNRF3 ectodomain crystal form II
4C99 2.8 Å, Mouse ZNRF3 ectodomain in complex with mouse RSPO2 Fu1-Fu2 crystal form I
4CDK 2.8 Å, Structure of ZNRF3-RSPO1
4C9E 3.0 Å, Mouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form II

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