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AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (B1LDZ1)

Analyse AlphaFold monomer V2.0 prediction for NH(3)-dependent NAD(+) synthetase (B1LDZ1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B1LDZ1
Type
protein
Length
275 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x0bA6797A653FEB253174C6e56A7ad3807e73357A
Molecule
NH(3)-dependent NAD(+) synthetase
UniProt
B1LDZ1
Pockets
2 · best druggability 0.82

Structure

1 distinct chain · 52% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANH(3)-dependent NAD(+) synthetaseprotein27552% helix, 8% strandB1LDZ1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15560.820.8863empty
2780.330.7415empty

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