Research workbench

Xenopus RSPO2 Fu1-Fu2 crystal form II

Analyse Xenopus RSPO2 Fu1-Fu2 crystal form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C8W
Type: protein
Length: 208 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.1
Source: XENOPUS (SILURANA) TROPICALIS
Molecule: R-spondin-2
UniProt: Q5M7L6
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · resolution 3.1 · 2 distinct chains · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
I	R-spondin-2	protein	104	0% helix, 48% strand	Q5M7L6
J	R-spondin-2	protein	104	0% helix, 51% strand	Q5M7L6

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.55	0.78	32	empty

Interfaces

1 interface between chains.

I–J · 448 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

4C8W · Xenopus RSPO2 FU1-FU2 crystal form II · the same entry in another collection · chain I against I, TM-score 1.00
Q5M7L6 · AlphaFold monomer V2.0 prediction for R-spondin-2 (Q5M7L6) · a predicted model of the same protein · chain J against A, TM-score 0.91

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5M7L6
Elsewhere: RCSB PDB 4C8W · PDBe 4C8W · UniProt Q5M7L6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.