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1MAW

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with ATP in an Open Conformation

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
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
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004830molecular_functiontryptophan-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006418biological_processtRNA aminoacylation for protein translation
C0006436biological_processtryptophanyl-tRNA aminoacylation
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004830molecular_functiontryptophan-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006418biological_processtRNA aminoacylation for protein translation
D0006436biological_processtryptophanyl-tRNA aminoacylation
E0000166molecular_functionnucleotide binding
E0004812molecular_functionaminoacyl-tRNA ligase activity
E0004830molecular_functiontryptophan-tRNA ligase activity
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006418biological_processtRNA aminoacylation for protein translation
E0006436biological_processtryptophanyl-tRNA aminoacylation
F0000166molecular_functionnucleotide binding
F0004812molecular_functionaminoacyl-tRNA ligase activity
F0004830molecular_functiontryptophan-tRNA ligase activity
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006418biological_processtRNA aminoacylation for protein translation
F0006436biological_processtryptophanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ATP A 400
ChainResidue
AGLY17
ASER196
AASN18
AGLY21
AALA22
AILE183
ALYS192
AMET193
ASER194
ALYS195

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ATP B 401
ChainResidue
BTHR15
BGLY17
BASN18
BGLY21
BILE183
BLYS192
BMET193
BSER194
BLYS195
BSER196

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ATP D 402
ChainResidue
DASN18
DGLY21
DPRO142
DPRO177
DILE183
DLYS192
DMET193
DSER194
DLYS195

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP E 403
ChainResidue
ETHR15
EGLY17
EASN18
EGLY21
EPRO177
EALA181
EILE183
ELYS192
EMET193
ESER194
ELYS195
ESER196

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ATP C 404
ChainResidue
CGLY17
CASN18
CALA22
CGLY144
CILE183
CLYS192
CMET193
CSER194
CLYS195
CSER196

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ATP F 405
ChainResidue
FTHR15
FGLY17
FASN18
FGLY21
FGLY144
FPRO177
FILE183
FLYS192
FMET193
FSER194
FLYS195
FSER196

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGvITIGNY
ChainResidueDetails
APRO10-TYR19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26555258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DK4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS192
ALYS195

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS192
BLYS195

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
CLYS192
CLYS195

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
DLYS192
DLYS195

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ELYS192
ELYS195

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
FLYS192
FLYS195

site_idMCSA1
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ALYS111electrostatic stabiliser
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
BLYS111electrostatic stabiliser
BLYS192electrostatic stabiliser
BLYS195electrostatic stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
CLYS111electrostatic stabiliser
CLYS192electrostatic stabiliser
CLYS195electrostatic stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
DLYS111electrostatic stabiliser
DLYS192electrostatic stabiliser
DLYS195electrostatic stabiliser

site_idMCSA5
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ELYS111electrostatic stabiliser
ELYS192electrostatic stabiliser
ELYS195electrostatic stabiliser

site_idMCSA6
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
FLYS111electrostatic stabiliser
FLYS192electrostatic stabiliser
FLYS195electrostatic stabiliser

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PDB entries from 2026-04-01

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