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AlphaFold monomer V2.0 prediction for putative polysaccharide biosynthesis protein with aminopeptidase-like domain (Q97H19)

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

Accession: Q97H19
Type: protein
Length: 434 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xE506F93E4458Acac5054741df112b789e99Fb9c6
Molecule: Putative polysaccharide biosynthesis protein with aminopeptidase-like domain
UniProt: Q97H19
Pockets: 3 · best druggability 0.37

Structure

1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative polysaccharide biosynthesis protein with aminopeptidase-like domain	protein	434	34% helix, 24% strand	Q97H19

Pockets

3 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	60	0.37	0.79	13	empty
2	84	0.36	0.76	20	empty
3	56	0.28	0.74	15	empty

Compared structures

3K9T · Crystal structure of putative peptidase (NP_348812.1) from CLOSTRIDIUM ACETOBUTYLICUM at… · an experimental structure of the same protein · chain A against A, TM-score 0.97
3K9T · Crystal structure of putative peptidase (NP_348812.1) from clostridium acetobutylicum at… · an experimental structure of the same protein · chain A against A, TM-score 0.97

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 Q97H19
Elsewhere: UniProt Q97H19 · AlphaFold DB Q97H19

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