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6JJ1

Crystal structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii at 0.97 A resolution with disordered five N-terminal residues

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 Residues3
Detailsbinding site for residue CL A 201
ChainResidue
AHIS94
AARG131
AHOH356

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 202
ChainResidue
AASN12
AHIS22
AASN116

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 203
ChainResidue
AARG133

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 204
ChainResidue
AHOH333
AHOH432
AGLU30
AHOH304

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

245663

PDB entries from 2025-12-03

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