4C8F: Mouse ZNRF3 ectodomain crystal form IV

Name: PDB 4C8F: mouse ZNRF3 ectodomain crystal form IV
Published: 2013-11-20
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

mouse ZNRF3 ectodomain crystal form IV. Determined by X-ray diffraction at 2.69 Å resolution. Released 20 Nov 2013.

Method: X-ray diffraction
Resolution: 2.69 Å
Organism: MUS MUSCULUS
Chains: 4
Atoms: 4,174
Mol. weight: 72.81 kDa
Released: 20 Nov 2013

Explore 4C8F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C8F contains 16 α-helices and 33 β-strands across 4 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: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	55-65	11	1
β-strand	71-82	12	1
β-strand	91-97	7	1
β-strand	117-122	6	1
α-helix	123-125	3
α-helix	136-145	10
β-strand	150-154	5	1
α-helix	160-165	6
β-strand	177-180	4	1
α-helix	182-194	13
β-strand	199-203	5	1

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	55-64	10	2
β-strand	71-82	12	2
β-strand	91-97	7	2
β-strand	117-121	5	2
α-helix	136-145	10
β-strand	150-154	5	2
α-helix	161-167	7
β-strand	177-180	4	2
α-helix	182-194	13
β-strand	200-203	4	2

Chain C: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	55-65	11	1
β-strand	71-82	12	1
β-strand	86	1	3
β-strand	91-98	8	1
β-strand	117-122	6	1
α-helix	123-125	3
α-helix	136-145	10
β-strand	148-154	7	1
α-helix	161-166	6
β-strand	173	1	3
β-strand	177-180	4	1
α-helix	182-192	11
β-strand	199-203	5	1

Chain D: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	55-56	2
β-strand	57-65	9	2
β-strand	71-79	9	2
β-strand	81-82	2	2
β-strand	86	1	4
β-strand	91-97	7	2
β-strand	117-122	6	2
α-helix	136-145	10
β-strand	150-154	5	2
α-helix	161-165	5
α-helix	166-168	3
β-strand	173	1	4
β-strand	177-180	4	2
α-helix	182-194	13
β-strand	198-203	6	2

Molecules and chains

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

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

>4C8F_1 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 (chains A, B, C, D)
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
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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