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8AXP

Neisseria gonorrhoeae peptidyl-tRNA hydrolase complexed with an XChem hit.

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
B0000049molecular_functiontRNA binding
B0003723molecular_functionRNA binding
B0004045molecular_functionpeptidyl-tRNA hydrolase activity
B0005737cellular_componentcytoplasm
B0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
B0016787molecular_functionhydrolase activity
B0072344biological_processrescue of stalled ribosome
Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YeqTRHNaGfwFLD
ChainResidueDetails
BTYR18-ASP31

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GnggHNGLKDI
ChainResidueDetails
BGLY112-ILE122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
BHIS23
AHIS23

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
BTYR18
BPHE69
BASN71
BASN117
ATYR18
APHE69
AASN71
AASN117

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Discriminates between blocked and unblocked aminoacyl-tRNA => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
BASN13
AASN13

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Stabilizes the basic form of H active site to accept a proton => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
BASP96
AASP96

237992

PDB entries from 2025-06-25

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