4C99: Mouse ZNRF3 ectodomain

Mouse ZNRF3 ectodomain in complex with mouse RSPO2 Fu1-Fu2 crystal form I. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Nov 2013.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: MUS MUSCULUS
Chains: 4
Atoms: 3,968
Mol. weight: 64.76 kDa
Released: 20 Nov 2013

Explore 4C99 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C99 contains 15 α-helices and 49 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: 6 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	91-97	7	1
α-helix	100-102	3
β-strand	118-122	5	1
α-helix	126-128	3
α-helix	136-145	10
β-strand	150-154	5	1
α-helix	160-166	7
α-helix	171-172	2
β-strand	173	1	2
β-strand	177-180	4	1
α-helix	182-194	13
β-strand	199-203	5	1

Chain B: 0 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	43-45	3	3
β-strand	51-52	2	4
β-strand	53-55	3	3
β-strand	60-66	7	4
β-strand	69-75	7	4
β-strand	82-83	2	5
β-strand	86	1	6
β-strand	91	1	6
β-strand	92	1	4
β-strand	94-95	2	5
β-strand	103	1	5
β-strand	112	1	5
β-strand	118-120	3	7
β-strand	123-125	3	7
β-strand	135	1	8
β-strand	140	1	8

Chain C: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	55-65	11	9
β-strand	71-82	12	9
β-strand	86	1	10
β-strand	91-97	7	9
α-helix	100-102	3
β-strand	117-122	6	9
α-helix	123-125	3
α-helix	126-128	3
α-helix	136-145	10
β-strand	148-154	7	9
α-helix	161-165	5
α-helix	166-168	3
β-strand	173	1	10
β-strand	177-180	4	9
α-helix	182-194	13
β-strand	199-204	6	9

Chain D: 2 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	11
β-strand	51-55	5	11
β-strand	60-61	2	12
β-strand	64-66	3	13
β-strand	69-71	3	13
β-strand	72	1	11
β-strand	74-75	2	12
β-strand	82-86	5	12
β-strand	91-95	5	12
β-strand	101-106	6	14
β-strand	109-113	5	14
α-helix	114	1
β-strand	118-120	3	15
β-strand	123-125	3	15
α-helix	128-129	2
β-strand	133-135	3	16
β-strand	140-142	3	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase ZNRF3	A, C	protein	165	MUS MUSCULUS	Q5SSZ7 (AlphaFold model)
R-spondin-2	B, D	protein	122	MUS MUSCULUS	Q8BFU0 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4C99_1 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 (chains A, C)
ETGKETAFVEVVLFESSPSGDYTTHTTGLTGRFSRAGAMLSAEGEIVQMHPLGLCNNNDE
EDLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGS
EDPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHLGTKHHHHHH

Sequence of entity 2 (B, D), FASTA

>4C99_2 R-SPONDIN-2 (chains B, D)
ETGNPICKGCLSCSKDNGCSRCQQKLFFFLRREGMRQYGECLHSCPSGYYGHRAPDMNRC
ARCRIENCDSCFSKDFCTKCKVGFYLHRGRCFDECPDGFAPLDETMECVEGTHHHHHHHH
HH

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
4C8A 2.7 Å, mouse ZNRF3 ectodomain crystal form II
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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