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AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit gamma (Q3T0K2)

Analyse AlphaFold monomer V2.0 prediction for T-complex protein 1 subunit gamma (Q3T0K2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q3T0K2
Type
protein
Length
545 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x5AF1007bEEe0CF438B019cDFeDD7CfAd3AB7afA8
Molecule
T-complex protein 1 subunit gamma
UniProt
Q3T0K2
Pockets
2 · best druggability 0.80

Structure

1 distinct chain · 49% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AT-complex protein 1 subunit gammaprotein54549% helix, 17% strandQ3T0K2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.800.9148empty
21430.450.7723empty

Compared structures

  • 3IYG · Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map · an experimental structure of the same protein · chain A against G, TM-score 0.87
  • 3IYG · Ca model of bovine TRIC/CCT derived from a 4.0 ångström cryo-EM MAP · an experimental structure of the same protein · chain A against G, TM-score 0.87
  • 4B2T · The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning · an experimental structure of the same protein · chain A against G, TM-score 0.82
  • 4B2T · The crystal structures of the eukaryotic chaperonin cct reveal its functional partitioning · an experimental structure of the same protein · chain A against G, TM-score 0.82

Analyse

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