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AlphaFold monomer V2.0 prediction for rhamnulose-1-phosphate aldolase (B5XZ54)

Analyse AlphaFold monomer V2.0 prediction for rhamnulose-1-phosphate aldolase (B5XZ54) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B5XZ54
Type
protein
Length
276 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x38047ce090cAC00B9195040abFba84F85133149B
Molecule
Rhamnulose-1-phosphate aldolase
UniProt
B5XZ54
Pockets
1 · best druggability 0.30

Structure

1 distinct chain · 46% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhamnulose-1-phosphate aldolaseprotein27646% helix, 17% strandB5XZ54

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.300.7319empty

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