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3NEA

Crystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensis

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 cytosolic ribosome
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 500
ChainResidue
ASER101
AGLN158

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
APHE40
ASER42
AASN49
ALYS108
AGLY109
AASP129

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AGLY114
AVAL146
AHOH214
AHOH216
AHOH218
AHIS22

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 512
ChainResidue
AASP35
AASN36
AHIS142
AILE170

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 513
ChainResidue
ALYS5
AASP56
ATYR57
ATYR83
APRO140
ALYS145

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 514
ChainResidue
AASN43
APRO44
ALYS45

Functional Information from PROSITE/UniProt
site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLRSI
ChainResidueDetails
AGLY111-ILE121

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

250359

PDB entries from 2026-03-11

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