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6WQX

Human PRPK-TPRKB complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000408cellular_componentEKC/KEOPS complex
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008033biological_processtRNA processing
A0019901molecular_functionprotein kinase binding
A1990145biological_processmaintenance of translational fidelity
B0000408cellular_componentEKC/KEOPS complex
B0002949biological_processtRNA threonylcarbamoyladenosine modification
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008033biological_processtRNA processing
B0019901molecular_functionprotein kinase binding
B1990145biological_processmaintenance of translational fidelity
C0000166molecular_functionnucleotide binding
C0000408cellular_componentEKC/KEOPS complex
C0002039molecular_functionp53 binding
C0003824molecular_functioncatalytic activity
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006468biological_processprotein phosphorylation
C0008033biological_processtRNA processing
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016787molecular_functionhydrolase activity
C0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
C0106310molecular_functionprotein serine kinase activity
C1901796biological_processregulation of signal transduction by p53 class mediator
C1990145biological_processmaintenance of translational fidelity
D0000166molecular_functionnucleotide binding
D0000408cellular_componentEKC/KEOPS complex
D0002039molecular_functionp53 binding
D0003824molecular_functioncatalytic activity
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006468biological_processprotein phosphorylation
D0008033biological_processtRNA processing
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0016787molecular_functionhydrolase activity
D0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
D0106310molecular_functionprotein serine kinase activity
D1901796biological_processregulation of signal transduction by p53 class mediator
D1990145biological_processmaintenance of translational fidelity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue ANP C 301
ChainResidue
CLYS40
CASN167
CLEU169
CILE182
CASP183
CMG302
CMG303
CHOH404
CHOH408
CVAL47
CLYS60
CPRO99
CMET113
CGLU114
CGLU115
CILE116
CSER166

site_idAC2
Number of Residues3
Detailsbinding site for residue MG C 302
ChainResidue
CASN167
CASP183
CANP301

site_idAC3
Number of Residues2
Detailsbinding site for residue MG C 303
ChainResidue
CASP183
CANP301

site_idAC4
Number of Residues15
Detailsbinding site for residue ANP D 301
ChainResidue
DLYS40
DVAL47
DLYS60
DPRO99
DMET113
DGLU114
DGLU115
DILE116
DTHR121
DSER166
DASN167
DLEU169
DILE182
DASP183
DMG302

site_idAC5
Number of Residues3
Detailsbinding site for residue MG D 302
ChainResidue
DASN167
DASP183
DANP301

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LIHgDLTTSNMLL
ChainResidueDetails
CLEU158-LEU170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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