4C8A: Mouse ZNRF3 ectodomain crystal form II

Name: PDB 4C8A: mouse ZNRF3 ectodomain crystal form II
Published: 2013-11-20
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

mouse ZNRF3 ectodomain crystal form II. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 Nov 2013.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: MUS MUSCULUS
Chains: 3
Atoms: 3,129
Mol. weight: 54.61 kDa
Released: 20 Nov 2013

Explore 4C8A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C8A contains 16 α-helices and 28 β-strands across 3 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: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	55-65	11	1
β-strand	71-82	12	1
β-strand	86	1	2
β-strand	91-98	8	1
α-helix	100-102	3
β-strand	117-122	6	1
α-helix	126-128	3
α-helix	136-145	10
β-strand	148-154	7	1
α-helix	160-166	7
β-strand	173	1	2
β-strand	177-180	4	1
α-helix	182-193	12
β-strand	199-204	6	1

Chain B: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	55-63	9	3
β-strand	73-82	10	3
β-strand	86	1	4
β-strand	91-98	8	3
α-helix	100-102	3
β-strand	117-122	6	3
α-helix	123-124	2
α-helix	126-128	3
α-helix	136-145	10
β-strand	148-154	7	3
α-helix	160-164	5
β-strand	173	1	4
β-strand	177-180	4	3
α-helix	182-193	12
β-strand	199-203	5	3

Chain C: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	55	1	5
β-strand	56-65	10	6
β-strand	71-78	8	6
β-strand	81-82	2	5
β-strand	91-94	4	6
β-strand	95-97	3	5
β-strand	118-122	5	5
α-helix	123-125	3
α-helix	126-128	3
α-helix	136-145	10
β-strand	150-154	5	5
α-helix	160-166	7
β-strand	177-180	4	5
α-helix	182-194	13
β-strand	198-204	7	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase ZNRF3	A, B, C	protein	165	MUS MUSCULUS	Q5SSZ7 (AlphaFold model)

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

>4C8A_1 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 (chains A, B, C)
ETGKETAFVEVVLFESSPSGDYTTHTTGLTGRFSRAGAMLSAEGEIVQMHPLGLCNNNDE
EDLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGS
EDPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHLGTKHHHHHH

Primary citation

Structural and Molecular Basis of Znrf3/Rnf43 Transmembrane Ubiquitin Ligase Inhibition by the Wnt Agonist R-Spondin. Zebisch, M., Xu, Y., Krastev, C. et al. Nat Commun (2013) 4:2787. DOI 10.1038/NCOMMS3787 · PubMed

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

4CDJ 1.5 Å, Structure of ZNRF3 ectodomain
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
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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