6CKX

Structure of CDK12/CycK in complex with a small molecule inhibitor N-(4-(1-methyl-1H-pyrazol-4-yl)phenyl)-N-((1r,4r)-4-(quinazolin-2-ylamino)cyclohexyl)acetamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0006357	biological_process	regulation of transcription by RNA polymerase II
D	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 1101

Chain	Residue
A	ASN864
A	ASP877
A	HOH1201

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site_id	AC2
Number of Residues	9
Details	binding site for residue 8M1 A 1102

Chain	Residue
A	HIS818
A	ASP819
A	LEU866
A	ILE732
A	ILE733
A	GLY734
A	ALA754
A	PHE813
A	MET816

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site_id	AC3
Number of Residues	1
Details	binding site for residue MG B 301

Chain	Residue
B	GLU158

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site_id	AC4
Number of Residues	2
Details	binding site for residue MG C 1101

Chain	Residue
C	ASN864
C	ASP877

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site_id	AC5
Number of Residues	10
Details	binding site for residue 8M1 C 1102

Chain	Residue
C	ILE732
C	ILE733
C	GLY734
C	GLU735
C	PHE813
C	GLU814
C	MET816
C	ASP817
C	ASP819
C	LEU866

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGQVYkAkdkdtgel..........VALK

Chain	Residue	Details
A	ILE733-LYS756

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

Chain	Residue	Details
A	PHE855-LEU867

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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:PRU10027

Chain	Residue	Details
A	ASP859
C	ASP859

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	GLU814
A	HIS1040
C	ILE733
C	LYS756
C	GLU814
C	HIS1040
A	ILE733
A	LYS756

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER889
C	SER889

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:24662513, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	TPO893
C	TPO893

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER1053
C	SER1053

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