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4OLJ

Crystal structure of Arg119Gln mutant of Peptidyl-tRNA Hydrolase from Acinetobacter Baumannii at 1.49 A resolution

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 PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AGLY14
APHE26
AGLU30
AMET66
AHOH311
AHOH367
AHOH500

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TLA A 202
ChainResidue
AMET69
AASN70
AASN116
AHOH483
AHOH489
AASN12
AHIS22

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaqTRHNaGfwFVE
ChainResidueDetails
ATYR17-GLU30

247536

PDB entries from 2026-01-14

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