4C8V: Xenopus RSPO2 Fu1-Fu2 crystal form I

Xenopus RSPO2 Fu1-Fu2 crystal form I. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Nov 2013.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: XENOPUS (SILURANA) TROPICALIS
Chains: 8
Atoms: 7,099
Mol. weight: 110.25 kDa
Released: 20 Nov 2013

Explore 4C8V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C8V contains 20 α-helices and 108 β-strands across 8 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, 13 β-strands

Element	Residues	Length	Sheet
α-helix	37-39	3
β-strand	43-46	4	1
β-strand	51	1	2
β-strand	52-55	4	1
β-strand	60-66	7	2
β-strand	69-75	7	2
α-helix	78-79	2
β-strand	82-86	5	2
β-strand	91-95	5	2
β-strand	101-106	6	3
β-strand	109-113	5	3
α-helix	114	1
β-strand	118-120	3	4
β-strand	123-125	3	4
α-helix	128-129	2
β-strand	132-135	4	4
β-strand	140-143	4	4

Chain B: 2 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	43	1	5
β-strand	46	1	6
β-strand	51	1	7
β-strand	52	1	6
β-strand	55	1	5
β-strand	60-66	7	7
β-strand	69-75	7	7
α-helix	78-79	2
β-strand	82-86	5	7
β-strand	91-95	5	7
β-strand	101-104	4	8
β-strand	110-113	4	8
α-helix	114	1
β-strand	118-120	3	9
β-strand	123-125	3	9
β-strand	132-135	4	9
β-strand	140-143	4	9

Chain C: 2 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	43	1	10
β-strand	46	1	11
β-strand	51	1	12
β-strand	52	1	11
β-strand	55	1	10
β-strand	60-66	7	12
β-strand	69-75	7	12
α-helix	78-79	2
β-strand	82-86	5	12
β-strand	91-95	5	12
β-strand	101-106	6	13
β-strand	109-113	5	13
α-helix	114	1
β-strand	118-120	3	14
β-strand	123-125	3	14
β-strand	132-135	4	14
β-strand	140-143	4	14

Chain D: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	43-46	4	15
β-strand	51	1	16
β-strand	52-55	4	15
β-strand	60-64	5	16
β-strand	71-75	5	16
α-helix	78-79	2
β-strand	82-86	5	16
β-strand	91-95	5	16
β-strand	101-106	6	17
β-strand	109-113	5	17
α-helix	114	1
β-strand	118-120	3	18
β-strand	123-125	3	18
α-helix	128-129	2
β-strand	132-135	4	18
β-strand	140-143	4	18

Chain E: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	19
β-strand	51-55	5	19
β-strand	60-64	5	19
β-strand	71-75	5	19
α-helix	78-79	2
β-strand	82-85	4	19
β-strand	91-95	5	19
β-strand	101-106	6	20
β-strand	109-113	5	20
β-strand	118-120	3	21
β-strand	123-125	3	21
α-helix	128-129	2
β-strand	133-134	2	22
β-strand	140	1	21
β-strand	141-142	2	22

Chain F: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	23
β-strand	51-55	5	23
β-strand	60-66	7	23
β-strand	69-75	7	23
α-helix	78-79	2
β-strand	82-86	5	23
β-strand	91-95	5	23
β-strand	101-106	6	24
β-strand	109-113	5	24
α-helix	117	1
β-strand	118-120	3	25
β-strand	123-125	3	25
α-helix	128-129	2
β-strand	133-134	2	26
β-strand	140	1	25
β-strand	141-142	2	26

Chain G: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	27
β-strand	51-55	5	27
β-strand	60-66	7	27
β-strand	69-75	7	27
α-helix	78-79	2
β-strand	82-86	5	27
β-strand	91-95	5	27
β-strand	101-104	4	28
β-strand	110-113	4	28
α-helix	114	1
β-strand	118-120	3	29
β-strand	123-125	3	29
β-strand	133-134	2	30
β-strand	140	1	29
β-strand	141-142	2	30

Chain H: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	43-47	5	31
β-strand	51-55	5	31
β-strand	60-66	7	31
β-strand	69-75	7	31
α-helix	78-79	2
β-strand	82-86	5	31
β-strand	91-95	5	31
β-strand	101-106	6	32
β-strand	109-113	5	32
α-helix	117	1
β-strand	118-120	3	33
β-strand	123-125	3	33
β-strand	133-134	2	34
β-strand	140	1	33
β-strand	141-142	2	34

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
R-spondin-2	A, B, C, D, E, F, G, H	protein	121	XENOPUS (SILURANA) TROPICALIS	Q5M7L6 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>4C8V_1 R-SPONDIN-2 (chains A, B, C, D, E, F, G, H)
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
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
4C8W 3.1 Å, Xenopus RSPO2 Fu1-Fu2 crystal form II

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