9D8U

Crystal structure of CDK6 in complex with atirmociclib

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000166	molecular_function	nucleotide binding
A	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
A	0001726	cellular_component	ruffle
A	0001954	biological_process	positive regulation of cell-matrix adhesion
A	0002244	biological_process	hematopoietic progenitor cell differentiation
A	0003323	biological_process	type B pancreatic cell development
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	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0006974	biological_process	DNA damage response
A	0007165	biological_process	signal transduction
A	0007219	biological_process	Notch signaling pathway
A	0008285	biological_process	negative regulation of cell population proliferation
A	0009615	biological_process	response to virus
A	0010389	biological_process	regulation of G2/M transition of mitotic cell cycle
A	0010468	biological_process	regulation of gene expression
A	0010628	biological_process	positive regulation of gene expression
A	0014002	biological_process	astrocyte development
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0021542	biological_process	dentate gyrus development
A	0021670	biological_process	lateral ventricle development
A	0030097	biological_process	hemopoiesis
A	0030154	biological_process	cell differentiation
A	0030332	molecular_function	cyclin binding
A	0033077	biological_process	T cell differentiation in thymus
A	0042063	biological_process	gliogenesis
A	0042995	cellular_component	cell projection
A	0043697	biological_process	cell dedifferentiation
A	0045596	biological_process	negative regulation of cell differentiation
A	0045638	biological_process	negative regulation of myeloid cell differentiation
A	0045646	biological_process	regulation of erythrocyte differentiation
A	0045656	biological_process	negative regulation of monocyte differentiation
A	0045668	biological_process	negative regulation of osteoblast differentiation
A	0045786	biological_process	negative regulation of cell cycle
A	0048146	biological_process	positive regulation of fibroblast proliferation
A	0048699	biological_process	generation of neurons
A	0050680	biological_process	negative regulation of epithelial cell proliferation
A	0051301	biological_process	cell division
A	0051726	biological_process	regulation of cell cycle
A	0060218	biological_process	hematopoietic stem cell differentiation
A	0097131	cellular_component	cyclin D1-CDK6 complex
A	0097132	cellular_component	cyclin D2-CDK6 complex
A	0097133	cellular_component	cyclin D3-CDK6 complex
A	0098770	molecular_function	FBXO family protein binding
A	0106310	molecular_function	protein serine kinase activity
A	1902036	biological_process	regulation of hematopoietic stem cell differentiation
A	2000145	biological_process	regulation of cell motility
A	2000773	biological_process	negative regulation of cellular senescence

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE19-LYS43

---

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

Chain	Residue	Details
A	VAL141-VAL153

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---