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AlphaFold monomer V2.0 prediction for secretory phospholipase A2 receptor (Q13018)

Analyse AlphaFold monomer V2.0 prediction for secretory phospholipase A2 receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q13018
Type: protein
Length: 1,463 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x537bb4F577545b8d4b420E3C42f972266e32e41D
Molecule: Secretory phospholipase A2 receptor
UniProt: Q13018
Pockets: 16 · best druggability 0.81

Structure

1 distinct chain · 18% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Secretory phospholipase A2 receptor	protein	1463	18% helix, 29% strand	Q13018

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1110	0.81	0.82	102	empty
2	1183	0.79	0.81	89	empty
3	679	0.74	0.80	70	empty
4	507	0.65	0.77	37	empty
5	403	0.61	0.77	50	empty

Modifications

Observed in the structure: 27 disulfide (disulfide).

Compared structures

7QSR · CryoEM structure of the Ectodomain of Human PLA2R · an experimental structure of the same protein · chain A against A, TM-score 0.64
6JLI · Crystal structure of CTLD7 domain of human PLA2R · an experimental structure of the same protein · chain A against A, TM-score 0.08
6JLI · Crystal structure of CTLD7 domain of human PLA2R · an experimental structure of the same protein · chain A against A, TM-score 0.08

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 Q13018
Elsewhere: UniProt Q13018 · AlphaFold DB Q13018

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