6WQX

Human PRPK-TPRKB complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000408	cellular_component	EKC/KEOPS complex
A	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008033	biological_process	tRNA processing
A	0019901	molecular_function	protein kinase binding
B	0000408	cellular_component	EKC/KEOPS complex
B	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008033	biological_process	tRNA processing
B	0019901	molecular_function	protein kinase binding
C	0000408	cellular_component	EKC/KEOPS complex
C	0002039	molecular_function	p53 binding
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006468	biological_process	protein phosphorylation
C	0008033	biological_process	tRNA processing
C	0016787	molecular_function	hydrolase activity
C	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
C	0106310	molecular_function	protein serine kinase activity
C	1901796	biological_process	regulation of signal transduction by p53 class mediator
D	0000408	cellular_component	EKC/KEOPS complex
D	0002039	molecular_function	p53 binding
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006468	biological_process	protein phosphorylation
D	0008033	biological_process	tRNA processing
D	0016787	molecular_function	hydrolase activity
D	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
D	0106310	molecular_function	protein serine kinase activity
D	1901796	biological_process	regulation of signal transduction by p53 class mediator

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ANP C 301

Chain	Residue
C	LYS40
C	ASN167
C	LEU169
C	ILE182
C	ASP183
C	MG302
C	MG303
C	HOH404
C	HOH408
C	VAL47
C	LYS60
C	PRO99
C	MET113
C	GLU114
C	GLU115
C	ILE116
C	SER166

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site_id	AC2
Number of Residues	3
Details	binding site for residue MG C 302

Chain	Residue
C	ASN167
C	ASP183
C	ANP301

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site_id	AC3
Number of Residues	2
Details	binding site for residue MG C 303

Chain	Residue
C	ASP183
C	ANP301

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site_id	AC4
Number of Residues	15
Details	binding site for residue ANP D 301

Chain	Residue
D	LYS40
D	VAL47
D	LYS60
D	PRO99
D	MET113
D	GLU114
D	GLU115
D	ILE116
D	THR121
D	SER166
D	ASN167
D	LEU169
D	ILE182
D	ASP183
D	MG302

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site_id	AC5
Number of Residues	3
Details	binding site for residue MG D 302

Chain	Residue
D	ASN167
D	ASP183
D	ANP301

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Functional Information from PROSITE/UniProt

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LIHgDLTTSNMLL

Chain	Residue	Details
C	LEU158-LEU170

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
C	ASP162
D	ASP162

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
D	VAL39
D	LYS60
C	LYS60
C	VAL39

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
D	SER34
C	SER34

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195

Chain	Residue	Details
D	THR135
C	THR135

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