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1GSG

Structure of E.coli glutaminyl-tRNA synthetase complexed with trnagln and ATP at 2.8 Angstroms resolution

Functional Information from GO Data
ChainGOidnamespacecontents
P0000166molecular_functionnucleotide binding
P0004812molecular_functionaminoacyl-tRNA ligase activity
P0004819molecular_functionglutamine-tRNA ligase activity
P0005524molecular_functionATP binding
P0005737cellular_componentcytoplasm
P0005829cellular_componentcytosol
P0006412biological_processtranslation
P0006418biological_processtRNA aminoacylation for protein translation
P0006424biological_processglutamyl-tRNA aminoacylation
P0006425biological_processglutaminyl-tRNA aminoacylation
P0016874molecular_functionligase activity
P0043039biological_processtRNA aminoacylation
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGyLHIGHA
ChainResidueDetails
PPRO33-ALA44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsRegion: {"description":"Interaction with tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12691748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15845536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZJW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00126","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18477696","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23727144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9562563","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1euy
ChainResidueDetails
PGLU34
PLYS270
PARG260

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1euy
ChainResidueDetails
PLYS270

site_idMCSA1
Number of Residues3
DetailsM-CSA 850
ChainResidueDetails

243083

PDB entries from 2025-10-15

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