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5UJJ

Crystal structure of human H130R tryptophanyl-tRNA synthetase in complex with TrpAMP

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
A0008285biological_processnegative regulation of cell population proliferation
A0016874molecular_functionligase activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030674molecular_functionprotein-macromolecule adaptor activity
A0032991cellular_componentprotein-containing complex
A0035556biological_processintracellular signal transduction
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
B0008285biological_processnegative regulation of cell population proliferation
B0016874molecular_functionligase activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030674molecular_functionprotein-macromolecule adaptor activity
B0032991cellular_componentprotein-containing complex
B0035556biological_processintracellular signal transduction
B0042803molecular_functionprotein homodimerization activity
B0045765biological_processregulation of angiogenesis
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue TYM A 501
ChainResidue
ATYR159
AGLU199
AGLN284
ACYS309
AALA310
AASP312
AGLN313
APHE317
ATHR338
APHE339
APHE340
ATHR160
ALYS349
AMET350
AMG502
AMG503
AHOH601
AHOH602
AHOH610
AHOH633
AGLY161
AARG162
AGLY163
AGLY172
AHIS173
APRO176
AGLN194

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
ALYS200
ATYM501
AMG503
AHOH635

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 503
ChainResidue
AARG162
AGLY163
ASER165
ATYM501
AMG502
AHOH602

site_idAC4
Number of Residues23
Detailsbinding site for residue TYM B 501
ChainResidue
BTYR159
BTHR160
BGLY161
BARG162
BGLY163
BGLY172
BHIS173
BPRO176
BGLN194
BGLU199
BGLN284
BCYS309
BALA310
BASP312
BGLN313
BPHE317
BPHE339
BPHE340
BLYS349
BMET350
BMG502
BHOH601
BHOH605

site_idAC5
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BASP312
BGLN313
BTYM501

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 Residues56
DetailsDomain: {"description":"WHEP-TRS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00531","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"1373391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P32921","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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