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AlphaFold monomer V2.0 prediction for endonuclease V (C3NMU5)

Analyse AlphaFold monomer V2.0 prediction for endonuclease V (C3NMU5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
C3NMU5
Type
protein
Length
198 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x046f0F60E30fEEae356021AFb4bFb96B4DC79519
Molecule
Endonuclease V
UniProt
C3NMU5
Pockets
2 · best druggability 0.47

Structure

1 distinct chain · 31% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndonuclease Vprotein19831% helix, 32% strandC3NMU5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11360.470.7825empty
2850.400.7716empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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