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2Z2I

Crystal structure of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0003723molecular_functionRNA binding
A0004045molecular_functionpeptidyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
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. YarTRHNlGfvVAD
ChainResidueDetails
ATYR17-ASP30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GeggHNGLRSV
ChainResidueDetails
AGLY111-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
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 Residues1
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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2pth
ChainResidueDetails
AHIS22
AASP95
AASN12

239149

PDB entries from 2025-07-23

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