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6WN2

Tyrosyl t-RNA Synthetase Mutant from E.coli Complexed with sulfotyrosine

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 Residues17
Detailsbinding site for residue TYS A 401
ChainResidue
ATYR37
AGLN179
AGLY182
ALEU186
AGLN201
AHOH524
AHOH550
AHOH568
AHOH581
AGLY39
APHE40
AASP41
AVAL71
AASP81
AASN126
APHE129
ATYR175

site_idAC2
Number of Residues6
Detailsbinding site for residue PG4 A 402
ChainResidue
AGLU88
AGLU164
AHOH528
AHOH557
BLYS144
BSER147

site_idAC3
Number of Residues4
Detailsbinding site for residue PG4 A 403
ChainResidue
AASP45
ATRP100
ATRP245
ALYS250

site_idAC4
Number of Residues6
Detailsbinding site for residue PG4 A 404
ChainResidue
AHIS145
APHE146
ASER147
AGLN150
AARG214
AHOH502

site_idAC5
Number of Residues3
Detailsbinding site for residue NA A 405
ChainResidue
ASO4408
AHOH582
AHOH593

site_idAC6
Number of Residues6
Detailsbinding site for residue NA A 406
ChainResidue
AILE79
AARG89
ALEU91
AGLU172
AHOH522
AHOH575

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 407
ChainResidue
ALYS85
AALA86
AALA87

site_idAC8
Number of Residues5
Detailsbinding site for residue SO4 A 408
ChainResidue
ALYS154
ATRP202
AGLY203
ATHR206
ANA405

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 A 409
ChainResidue
ATHR43
AHIS48
AARG89

site_idAD1
Number of Residues16
Detailsbinding site for residue TYS B 401
ChainResidue
BTYR37
BGLY39
BPHE40
BASP41
BVAL71
BASP81
BASN126
BTYR175
BGLN179
BGLY182
BLEU186
BGLN201
BHOH528
BHOH544
BHOH587
BHOH601

site_idAD2
Number of Residues3
Detailsbinding site for residue PG4 B 402
ChainResidue
ALYS295
BTRP245
BLYS250

site_idAD3
Number of Residues11
Detailsbinding site for residue PG4 B 403
ChainResidue
BHIS145
BPHE146
BSER147
BGLN150
BSER207
BASP210
BARG213
BARG214
BHOH501
BHOH524
BHOH579

site_idAD4
Number of Residues6
Detailsbinding site for residue NA B 404
ChainResidue
BILE79
BARG89
BLEU91
BGLU172
BHOH535
BHOH541

site_idAD5
Number of Residues5
Detailsbinding site for residue NA B 405
ChainResidue
BASN5
BALA26
BLEU29
BALA30
BHOH642

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 B 406
ChainResidue
BLYS85
BALA86
BALA87
BHOH507

site_idAD7
Number of Residues5
Detailsbinding site for residue SO4 B 407
ChainResidue
BTRP202
BTHR206
BHOH610
BHOH628
BLYS154

site_idAD8
Number of Residues3
Detailsbinding site for residue SO4 B 408
ChainResidue
BHIS48
BARG89
BHOH504

site_idAD9
Number of Residues4
Detailsbinding site for residue SO4 B 409
ChainResidue
BARG105
BLYS230
BGLY233
BHOH577

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

224004

PDB entries from 2024-08-21

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