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5TGT

Crystal structure of glytamyl-tRNA synthetase GluRS from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004818molecular_functionglutamate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006424biological_processglutamyl-tRNA aminoacylation
A0008270molecular_functionzinc ion binding
A0043039biological_processtRNA aminoacylation
A0046872molecular_functionmetal ion binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004818molecular_functionglutamate-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006424biological_processglutamyl-tRNA aminoacylation
B0008270molecular_functionzinc ion binding
B0043039biological_processtRNA aminoacylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue 2PE A 601
ChainResidue
AGLN339
ALEU348
BALA335
BGLN339
BLEU348
BMET349
BILE365

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 602
ChainResidue
ASER450
ASO4606
AHIS354
AARG358

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 603
ChainResidue
AALA446
ASER447
BARG432

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 604
ChainResidue
ATRP64
AGLU265
AGLU337
ATRP341
AHOH722

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 605
ChainResidue
ALYS188
ATHR194
ATYR195

site_idAC6
Number of Residues2
Detailsbinding site for residue SO4 A 606
ChainResidue
AGLY357
ASO4602

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 607
ChainResidue
ALYS340
ATRP341
AALA342
AASN344

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 A 608
ChainResidue
AILE23
AARG213
AGLY214
AGLU216
ATRP217

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 701
ChainResidue
BARG7
BILE8
BALA9
BGLY214
BGLU216
BTRP217

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 702
ChainResidue
AARG432
BHIS445
BALA446
BSER447

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 B 703
ChainResidue
BHIS354
BARG358
BSER450

site_idAD3
Number of Residues6
Detailsbinding site for residue SO4 B 704
ChainResidue
BTRP64
BGLU265
BTYR269
BPRO271
BTRP341
BHOH805

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 B 705
ChainResidue
BLYS188
BTHR194
BTYR195
BHOH808

site_idAD5
Number of Residues6
Detailsbinding site for residue SO4 B 706
ChainResidue
BLYS340
BTRP341
BALA342
BASN344
BTYR347
BHOH823

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 B 707
ChainResidue
BGLN399
BARG468
BGLU472
BHOH814

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGdPHVGTA
ChainResidueDetails
APRO10-ALA21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00022
ChainResidueDetails
ACYS107
BLYS254
ACYS109
ACYS134
AHIS136
ALYS254
BCYS107
BCYS109
BCYS134
BHIS136

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PDB entries from 2024-07-10

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