4C8W: Xenopus RSPO2 Fu1-Fu2 crystal form II

Xenopus RSPO2 Fu1-Fu2 crystal form II. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 Nov 2013.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: XENOPUS (SILURANA) TROPICALIS
Chains: 2
Atoms: 1,549
Mol. weight: 27.56 kDa
Released: 20 Nov 2013

Explore 4C8W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C8W contains 3 α-helices and 25 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 I: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	1
β-strand	51-55	5	1
β-strand	60-65	6	1
β-strand	70-75	6	1
β-strand	82-86	5	1
β-strand	91-95	5	1
β-strand	101-106	6	2
β-strand	109-113	5	2
α-helix	114	1
β-strand	118-120	3	3
β-strand	123-125	3	3
β-strand	140	1	3

Chain J: 2 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	43	1	4
β-strand	46-47	2	5
β-strand	51-52	2	5
β-strand	55	1	4
β-strand	60-66	7	6
β-strand	69-75	7	6
α-helix	78-79	2
β-strand	82-86	5	6
β-strand	91-95	5	6
β-strand	101-106	6	7
β-strand	109-113	5	7
α-helix	114	1
β-strand	118-120	3	8
β-strand	123-125	3	8
β-strand	133-135	3	8
β-strand	140-142	3	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
R-spondin-2	I, J	protein	121	XENOPUS (SILURANA) TROPICALIS	Q5M7L6 (AlphaFold model)

Sequence of entity 1 (I, J), FASTA

>4C8W_1 R-SPONDIN-2 (chains I, J)
ETGGTNPICKGCLSCSKDNGCLRCQPKLFFYLRREGMRQYGECLQSCPPGYYGVRGPDMN
RCSRCRIENCDSCFSRDFCIKCKSGFYSHKGQCFEECPEGFAPLDDTMVCVDGTKHHHHH
H

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 Q5M7L6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4C9R 2.1 Å, Xenopus ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 crystal form I
4C8V 2.2 Å, Xenopus RSPO2 Fu1-Fu2 crystal form I
4C9A 2.4 Å, Mouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form I
4C9V 2.7 Å, Xenopus RNF43 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2
4C9E 3.0 Å, Mouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form II
4C9U 3.0 Å, Xenopus ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 crystal form II

Browse structure collections

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