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1M83

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with ATP in a Closed, Pre-transition State 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
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
A0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 500
ChainResidue
AGLN9
AATP400
AHOH634

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP A 400
ChainResidue
ALYS111
AVAL143
AGLY144
AASP146
AGLN147
AGLY180
AALA181
AARG182
AILE183
ALYS192
AMET193
ASER194
ALYS195
ASER196
AMG500
AHOH506
AHOH525
AGLN9
ASER11
AGLY17
AASN18
AGLY21
AALA22

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 920
ChainResidue
ASER11
ATRP48
AGLN49
AASP50
ASER196

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 930
ChainResidue
ALYS218
ATHR222
ATYR265
ALYS269

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 940
ChainResidue
AASN34
ACYS35
ATYR36
ATHR73
AGLN74
AALA75
ATHR76
ALYS215
ALYS306
AHOH571

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 Residues8
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00140","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
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_idMCSA1
Number of Residues3
DetailsM-CSA 481
ChainResidueDetails
ALYS111electrostatic stabiliser
ALYS192electrostatic stabiliser
ALYS195electrostatic stabiliser

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PDB entries from 2025-12-24

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