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5V0I

Crystal Structure of Tryptophanyl-tRNA Synthetase from Escherichia coli Complexed with AMP and Tryptophan

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue AMP A 401
ChainResidue
AGLY19
AHOH537
AASN20
AGLY23
APRO180
AALA184
AVAL186
ALYS195
AMET196
ALYS198

site_idAC2
Number of Residues8
Detailsbinding site for residue TRP A 402
ChainResidue
APHE7
AGLY9
AGLN11
AVAL42
AHIS45
AMET132
AASP135
AGLN150

site_idAC3
Number of Residues5
Detailsbinding site for residue FMT A 403
ChainResidue
AHIS36
AILE38
ATHR78
AHIS316
AHOH544

site_idAC4
Number of Residues3
Detailsbinding site for residue FMT A 404
ChainResidue
ATYR100
AARG106
BGLU119

site_idAC5
Number of Residues8
Detailsbinding site for residue AMP B 401
ChainResidue
BGLY19
BASN20
BASP149
BALA184
BVAL186
BLYS195
BMET196
BLYS198

site_idAC6
Number of Residues10
Detailsbinding site for residue TRP B 402
ChainResidue
BPHE7
BGLY9
BGLN11
BVAL42
BHIS45
BMET132
BASP135
BILE136
BGLN150
BHOH506

site_idAC7
Number of Residues4
Detailsbinding site for residue FMT B 403
ChainResidue
BHIS36
BILE38
BTHR78
BHIS316

site_idAC8
Number of Residues5
Detailsbinding site for residue FMT B 404
ChainResidue
ATYR98
ATYR100
AARG163
BARG50
BASN122

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGeLTIGNY
ChainResidueDetails
APRO12-TYR21

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140
ChainResidueDetails
AGLN11
BGLY147
BVAL186
BLYS195
AGLY19
AASP135
AGLY147
AVAL186
ALYS195
BGLN11
BGLY19
BASP135

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PDB entries from 2024-08-28

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