Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HZ7

Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004819molecular_functionglutamine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006424biological_processglutamyl-tRNA aminoacylation
A0006425biological_processglutaminyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A0016884molecular_functioncarbon-nitrogen ligase activity, with glutamine as amido-N-donor
A0043039biological_processtRNA aminoacylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1euy
ChainResidueDetails
ALYS311
AASP75
AARG301

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1euy
ChainResidueDetails
ALYS311

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon