Research workbench

AlphaFold monomer V2.0 prediction for epidermin decarboxylase (P30197)

Analyse AlphaFold monomer V2.0 prediction for epidermin decarboxylase (P30197) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P30197
Type: protein
Length: 181 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x2812091d14c5E88aE48Dfd1ab07A3FcA007DcbB5
Molecule: Epidermin decarboxylase
UniProt: P30197
Pockets: 2 · best druggability 0.45

Structure

1 distinct chain · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epidermin decarboxylase	protein	181	41% helix, 23% strand	P30197

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	146	0.45	0.76	24	empty
2	68	0.34	0.76	15	empty

Compared structures

1G5Q · Epid H67N complexed with substrate peptide dsytc · an experimental structure of the same protein · chain A against D, TM-score 0.96
1G5Q · Epid H67N complexed with substrate peptide dsytc · an experimental structure of the same protein · chain A against D, TM-score 0.96
1G63 · Peptidyl-cysteine decarboxylase epid · an experimental structure of the same protein · chain A against B, TM-score 0.92
1G63 · Peptidyl-cysteine decarboxylase epid · an experimental structure of the same protein · chain A against B, TM-score 0.92

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 P30197
Elsewhere: UniProt P30197 · AlphaFold DB P30197

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