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AlphaFold monomer V2.0 prediction for telomere length regulator TAZ1 (P79005)

Analyse AlphaFold monomer V2.0 prediction for telomere length regulator TAZ1 (P79005) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P79005
Type
protein
Length
663 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
Molecule
Telomere length regulator TAZ1
UniProt
P79005
Pockets
6 · best druggability 0.64

Structure

1 distinct chain · 53% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATelomere length regulator TAZ1protein66353% helix, 0% strandP79005

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.640.9413empty
24400.570.7438empty
32560.530.7524empty
41070.430.7816empty
5980.420.7823empty

Compared structures

  • 4ZMI · Crystal structure of the helical domain of S. pombe TAZ1 · an experimental structure of the same protein · chain A against A, TM-score 0.35
  • 4ZMK · Crystal structure of the dimerization domain of S. pombe Taz1 · an experimental structure of the same protein · chain A against A, TM-score 0.11
  • 4ZMK · Crystal structure of the dimerization domain of S. pombe TAZ1 · an experimental structure of the same protein · chain A against A, TM-score 0.11
  • 2L3N · Solution structure of Rap1-Taz1 fusion protein · an experimental structure of the same protein · chain A against A, TM-score 0.08
  • 2L3N · Solution structure of RAP1-TAZ1 fusion protein · an experimental structure of the same protein · chain A against A, TM-score 0.08

Analyse

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