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6I5Y

Crystal structure of E. coli tyrRS in complex with 5'-O-(N-L-tyrosyl)sulfamoyl-adenosine

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 PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue YSA A 501
ChainResidue
ATYR37
AASP81
ATYR175
AGLN179
AASP182
AGLN195
AGLY197
AGLY198
AASP200
AGLN201
APRO226
AGLY39
ALEU227
AILE228
AHOH601
AHOH630
AHOH641
AHOH642
AHOH651
AHOH701
AHOH844
AASP41
AGLY50
AHIS51
AVAL53
APRO54
ALEU71
ATHR76

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 502
ChainResidue
APRO110
APHE111
ALEU310
AVAL311
AHOH615

site_idAC3
Number of Residues26
Detailsbinding site for residue YSA B 501
ChainResidue
BTYR37
BGLY39
BASP41
BGLY50
BHIS51
BVAL53
BPRO54
BLEU71
BASP81
BTYR175
BGLN179
BASP182
BGLN195
BGLY197
BGLY198
BASP200
BGLN201
BLEU227
BILE228
BHOH602
BHOH625
BHOH646
BHOH648
BHOH719
BHOH778
BHOH819

site_idAC4
Number of Residues2
Detailsbinding site for residue EDO B 502
ChainResidue
BPRO33
BGLU118

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO B 503
ChainResidue
BILE386
BGLU389
BLYS390
BGLN391
BTYR396
BGLU402
BHOH693

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

224931

PDB entries from 2024-09-11

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