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1VBN

Escherichia coli tyrosyl-tRNA synthetase mutant complexed with Tyr-AMS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004831molecular_functiontyrosine-tRNA ligase activity
B0005524molecular_functionATP binding
B0006418biological_processtRNA aminoacylation for protein translation
B0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE YSA A 1001
ChainResidue
AGLY39
AGLN179
AASP182
AGLY198
AASP200
AGLN201
APRO226
ALEU227
AILE228
AHOH1010
AASP41
AGLY50
AHIS51
AVAL53
APRO54
ATHR76
AASP81
ATYR175

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE YSA B 1002
ChainResidue
BGLY39
BASP41
BGLY50
BHIS51
BVAL53
BPRO54
BLEU71
BASP81
BTYR175
BGLN179
BASP182
BGLY197
BGLY198
BASP200
BGLN201
BPRO226
BLEU227
BILE228

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
ACYS38
BCYS38

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
AASN176
AGLY180
BASN176
BGLY180

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02006
ChainResidueDetails
ATHR239
BTHR239

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cross-linked with tRNA by periodate oxidation
ChainResidueDetails
AASP232
ATHR239
BASP232
BTHR239

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cross-linked with tRNA by periodate oxidation; predominant
ChainResidueDetails
APHE236
BPHE236

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
AHIS145
BHIS145

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS238
ALYS235

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS238
BLYS235

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS85
ALYS238
ALYS235
AARG89

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS85
BLYS238
BLYS235
BARG89

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PDB entries from 2025-06-18

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