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4A91

Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate

Replaces:  2ZLZ
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002097biological_processtRNA wobble base modification
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004818molecular_functionglutamate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0006424biological_processglutamyl-tRNA aminoacylation
A0008270molecular_functionzinc ion binding
A0016874molecular_functionligase activity
A0043039biological_processtRNA aminoacylation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLU A 301
ChainResidue
AARG9
AHOH537
AALA11
ASER13
AGLU45
ATYR172
AARG190
ALEU194
AHOH488
AHOH425

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1295
ChainResidue
ACYS101
ACYS103
ATYR115
ACYS119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18602926","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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