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AlphaFold monomer V2.0 prediction for catalase-peroxidase (P9WIE5)

Analyse AlphaFold monomer V2.0 prediction for catalase-peroxidase (P9WIE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P9WIE5
Type
protein
Length
740 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
Molecule
Catalase-peroxidase
UniProt
P9WIE5
Pockets
13 · best druggability 0.86

Structure

1 distinct chain · 44% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACatalase-peroxidaseprotein74044% helix, 7% strandP9WIE5

Pockets

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13460.860.9549empty
24510.710.8137empty
36600.710.7861empty
4690.630.9219empty
5960.550.8530empty

Compared structures

  • 8DWR · Crystal structure of the L333V variant of catalase-peroxidase from Mycobacterium… · an experimental structure of the same protein · chain A against A, TM-score 0.97

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