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AlphaFold monomer V2.0 prediction for glycerophosphocholine phosphodiesterase GPCPD1 (Q9NPB8)

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

Accession: Q9NPB8
Type: protein
Length: 672 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
Molecule: Glycerophosphocholine phosphodiesterase GPCPD1
UniProt: Q9NPB8
Pockets: 10 · best druggability 0.70

Structure

1 distinct chain · 21% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerophosphocholine phosphodiesterase GPCPD1	protein	672	21% helix, 31% strand	Q9NPB8

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	321	0.70	0.84	36	empty
2	328	0.66	0.81	41	empty
3	563	0.64	0.75	52	empty
4	250	0.58	0.79	30	empty
5	242	0.57	0.78	31	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2Z0B · Crystal structure of CBM20 domain of human putative glycerophosphodiester… · an experimental structure of the same protein · chain A against D, TM-score 0.16
2Z0B · Crystal structure of CBM20 domain of human putative glycerophosphodiester… · an experimental structure of the same protein · chain A against D, TM-score 0.16

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 Q9NPB8
Elsewhere: UniProt Q9NPB8 · AlphaFold DB Q9NPB8

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