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7AP3

Crystal structure of E. coli tyrosyl-tRNA synthetase in complex with TyrS7HMDDA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
A0016020cellular_componentmembrane
A0042803molecular_functionprotein homodimerization activity
A0043039biological_processtRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004831molecular_functiontyrosine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006437biological_processtyrosyl-tRNA aminoacylation
B0016020cellular_componentmembrane
B0042803molecular_functionprotein homodimerization activity
B0043039biological_processtRNA aminoacylation
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHLGHL
ChainResidueDetails
APRO42-LEU52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000305|PubMed:15671170
ChainResidueDetails
ATYR37
BTYR37

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170, ECO:0000305|PubMed:20159998
ChainResidueDetails
ATYR175
AGLN179
BTYR175
BGLN179

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02006
ChainResidueDetails
ALYS238
BLYS238

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cross-linked with tRNA by periodate oxidation
ChainResidueDetails
AALA231
ALYS238
BALA231
BLYS238

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cross-linked with tRNA by periodate oxidation; predominant
ChainResidueDetails
ALYS235
BLYS235

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS144
BLYS144

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PDB entries from 2024-11-13

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