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2QUH

Crystal structures of human tryptophanyl-tRNA synthetase in complex with Trp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001525biological_processangiogenesis
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
A0006469biological_processnegative regulation of protein kinase activity
A0008285biological_processnegative regulation of cell population proliferation
A0010628biological_processpositive regulation of gene expression
A0016874molecular_functionligase activity
A0019210molecular_functionkinase inhibitor activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0031334biological_processpositive regulation of protein-containing complex assembly
A0032991cellular_componentprotein-containing complex
A0042803molecular_functionprotein homodimerization activity
A0045765biological_processregulation of angiogenesis
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0001525biological_processangiogenesis
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004830molecular_functiontryptophan-tRNA ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
B0006469biological_processnegative regulation of protein kinase activity
B0008285biological_processnegative regulation of cell population proliferation
B0010628biological_processpositive regulation of gene expression
B0016874molecular_functionligase activity
B0019210molecular_functionkinase inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0031334biological_processpositive regulation of protein-containing complex assembly
B0032991cellular_componentprotein-containing complex
B0042803molecular_functionprotein homodimerization activity
B0045765biological_processregulation of angiogenesis
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TRP B 817
ChainResidue
ATYR159
ACYS309
AGLN313
APHE317
ATHR160
AGLY161
AGLY163
AGLN194
ATHR196
AGLU199
ALYS200
AGLN284

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TRP B 818
ChainResidue
BTYR159
BTHR160
BGLY161
BARG162
BGLY163
BGLN194
BTHR196
BGLU199
BLYS200
BGLN284
BCYS309
BGLN313
BPHE317

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SEaMHVGHL
ChainResidueDetails
APRO164-LEU174

site_idPS00762
Number of Residues29
DetailsWHEP_TRS_1 WHEP-TRS domain signature. QGElVRslKagNAskdeIDsaVkmLvslK
ChainResidueDetails
AGLN19-LYS47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P32921","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
AALA352
ALYS349

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BALA352
BLYS349

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PDB entries from 2025-07-23

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