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AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase, mitochondrial (P11024)

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

Accession
P11024
Type
protein
Length
1,086 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x133E079e1cB0870fc07292176c48cFF7F4BEb7C7
Molecule
NAD(P) transhydrogenase, mitochondrial
UniProt
P11024
Pockets
11 · best druggability 0.79

Structure

1 distinct chain · 54% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANAD(P) transhydrogenase, mitochondrialprotein108654% helix, 10% strandP11024

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111730.790.81100empty
24820.730.8251empty
33230.580.7636empty
41220.470.7822empty
51330.460.7719empty

Compared structures

  • 1D4O · Crystal structure of transhydrogenase domain III at 1.2 ångströms resolution · an experimental structure of the same protein · chain A against A, TM-score 0.16
  • 1D4O · Crystal structure of transhydrogenase domain III at 1.2 ångströms resolution · an experimental structure of the same protein · chain A against A, TM-score 0.16

Analyse

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