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7EER

Crystal structure of Tryptophanyl-tRNA synthetase from Bacillus stearothermophilus in complex with 05E6 and ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004830molecular_functiontryptophan-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004830molecular_functiontryptophan-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006436biological_processtryptophanyl-tRNA aminoacylation
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004830molecular_functiontryptophan-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006418biological_processtRNA aminoacylation for protein translation
D0006436biological_processtryptophanyl-tRNA aminoacylation
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY
ChainResidueDetails
APRO10-TYR19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140, ECO:0000269|PubMed:26555258, ECO:0007744|PDB:5DK4
ChainResidueDetails
AGLN9
BGLY144
BILE183
BLYS192
CGLN9
CGLY17
CASP132
CGLY144
CILE183
CLYS192
DGLN9
AGLY17
DGLY17
DASP132
DGLY144
DILE183
DLYS192
AASP132
AGLY144
AILE183
ALYS192
BGLN9
BGLY17
BASP132

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ALYS111electrostatic stabiliser
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
BLYS111electrostatic stabiliser
BLYS192electrostatic stabiliser
BLYS195electrostatic stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
CLYS111electrostatic stabiliser
CLYS192electrostatic stabiliser
CLYS195electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
DLYS111electrostatic stabiliser
DLYS192electrostatic stabiliser
DLYS195electrostatic stabiliser

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PDB entries from 2024-06-26

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