Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8P6V

Cryo-EM structure of CAK in complex with inhibitor ICEC0942

Functional Information from GO Data

Chain	GOid	namespace	contents
I	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
I	0000439	cellular_component	transcription factor TFIIH core complex
I	0005515	molecular_function	protein binding
I	0005634	cellular_component	nucleus
I	0005654	cellular_component	nucleoplasm
I	0005675	cellular_component	transcription factor TFIIH holo complex
I	0006351	biological_process	DNA-templated transcription
I	0006357	biological_process	regulation of transcription by RNA polymerase II
I	0006367	biological_process	transcription initiation at RNA polymerase II promoter
I	0016251	molecular_function	RNA polymerase II general transcription initiation factor activity
I	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity
I	0050821	biological_process	protein stabilization
I	0070516	cellular_component	CAK-ERCC2 complex
I	0070985	cellular_component	transcription factor TFIIK complex
I	2000045	biological_process	regulation of G1/S transition of mitotic cell cycle
J	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
J	0000439	cellular_component	transcription factor TFIIH core complex
J	0001650	cellular_component	fibrillar center
J	0001673	cellular_component	male germ cell nucleus
J	0004672	molecular_function	protein kinase activity
J	0004674	molecular_function	protein serine/threonine kinase activity
J	0004693	molecular_function	cyclin-dependent protein serine/threonine kinase activity
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005634	cellular_component	nucleus
J	0005654	cellular_component	nucleoplasm
J	0005675	cellular_component	transcription factor TFIIH holo complex
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0005886	cellular_component	plasma membrane
J	0006281	biological_process	DNA repair
J	0006366	biological_process	transcription by RNA polymerase II
J	0006367	biological_process	transcription initiation at RNA polymerase II promoter
J	0006468	biological_process	protein phosphorylation
J	0008094	molecular_function	ATP-dependent activity, acting on DNA
J	0008353	molecular_function	RNA polymerase II CTD heptapeptide repeat kinase activity
J	0016301	molecular_function	kinase activity
J	0042795	biological_process	snRNA transcription by RNA polymerase II
J	0045944	biological_process	positive regulation of transcription by RNA polymerase II
J	0048471	cellular_component	perinuclear region of cytoplasm
J	0050821	biological_process	protein stabilization
J	0051301	biological_process	cell division
J	0051726	biological_process	regulation of cell cycle
J	0070516	cellular_component	CAK-ERCC2 complex
J	0070985	cellular_component	transcription factor TFIIK complex
J	0106310	molecular_function	protein serine kinase activity
J	0140833	molecular_function	RNA polymerase II CTD heptapeptide repeat Y1 kinase activity
J	0140834	molecular_function	RNA polymerase II CTD heptapeptide repeat S2 kinase activity
J	0140835	molecular_function	RNA polymerase II CTD heptapeptide repeat T4 kinase activity
J	0140836	molecular_function	RNA polymerase II CTD heptapeptide repeat S5 kinase activity
J	0140837	molecular_function	RNA polymerase II CTD heptapeptide repeat S7 kinase activity
J	2000045	biological_process	regulation of G1/S transition of mitotic cell cycle

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGQFATVYkArdkntnqiv.........AIKK

Chain	Residue	Details
J	LEU18-LYS42

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpnNLLL

Chain	Residue	Details
J	ILE133-LEU145

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027, ECO:0000269\|PubMed:15530371

Chain	Residue	Details
J	ASP137
I	SER304

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000269\|PubMed:15530371

Chain	Residue	Details
J	LEU18
J	LYS41

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
J	ALA2

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976

Chain	Residue	Details
J	SER7

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK1 and CDK2 => ECO:0000269\|PubMed:11113184, ECO:0000269\|PubMed:9832506, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
J	SER164

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CDK2 => ECO:0000269\|PubMed:11113184, ECO:0000269\|PubMed:15530371, ECO:0000269\|PubMed:9832506, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
J	THR170

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
J	SER321

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)