8H4R

The Crystal Structure of CDK3 and CyclinE1 Complex with Dinaciclib from Biortus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
A	0004364	molecular_function	glutathione transferase activity
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004693	molecular_function	cyclin-dependent protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006468	biological_process	protein phosphorylation
A	0006749	biological_process	glutathione metabolic process
A	0006974	biological_process	DNA damage response
A	0007165	biological_process	signal transduction
A	0008283	biological_process	cell population proliferation
A	0010389	biological_process	regulation of G2/M transition of mitotic cell cycle
A	0010468	biological_process	regulation of gene expression
A	0016310	biological_process	phosphorylation
A	0016740	molecular_function	transferase activity
A	0030332	molecular_function	cyclin binding
A	0045023	biological_process	G0 to G1 transition
A	0045746	biological_process	negative regulation of Notch signaling pathway
A	0051301	biological_process	cell division
A	0106310	molecular_function	protein serine kinase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE10-LYS33

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

Chain	Residue	Details
A	VAL123-ILE135

site_id	PS00292
Number of Residues	32
Details	CYCLINS Cyclins signature. RaiLldWLmevcevykLhretFylAQdFFDRY

Chain	Residue	Details
B	ARG145-TYR176

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18691976, ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	TYR-117

site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP127

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159