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6JGU

Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from Acinetobacter baumannii.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0003723molecular_functionRNA binding
A0004045molecular_functionpeptidyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
A0016787molecular_functionhydrolase activity
A0072344biological_processrescue of stalled ribosome
Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaqTRHNaGfwFVE
ChainResidueDetails
ATYR17-GLU30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLRDI
ChainResidueDetails
AGLY111-ILE121

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PDB entries from 2025-07-02

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