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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B3ECG5)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (B3ECG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B3ECG5
Type
protein
Length
190 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7782F4817b37743d738e9aF842bf74bd50f2015E
Molecule
Peptidyl-tRNA hydrolase
UniProt
B3ECG5

Structure

1 distinct chain · 44% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein19044% helix, 25% strandB3ECG5

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