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5EKT

Crystal structure of mutant-K146A of peptidyl-tRNA hydrolase from Vibrio cholerae at 1.63A 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
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 PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue FLC B 201
ChainResidue
AASN14
BASN72
BASN118
AHIS24
APHE70
AMET71
AASN118
BASN14
BHIS24
BPHE70
BMET71

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YakTRHNaGawVVE
ChainResidueDetails
ATYR19-GLU32

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLKDT
ChainResidueDetails
AGLY113-THR123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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