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AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q55CT0)

Analyse AlphaFold monomer V2.0 prediction for tripeptidyl-peptidase 1 (Q55CT0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q55CT0
Type
protein
Length
600 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
Molecule
Tripeptidyl-peptidase 1
UniProt
Q55CT0
Pockets
7 · best druggability 0.70

Structure

1 distinct chain · 29% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATripeptidyl-peptidase 1protein60029% helix, 20% strandQ55CT0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14390.700.8153empty
21290.480.7927empty
31330.450.7734empty
41370.440.7727empty
5990.400.7718empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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