1JVP

Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0000082	biological_process	G1/S transition of mitotic cell cycle
P	0000086	biological_process	G2/M transition of mitotic cell cycle
P	0000166	molecular_function	nucleotide binding
P	0000287	molecular_function	magnesium ion binding
P	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
P	0000781	cellular_component	chromosome, telomeric region
P	0000793	cellular_component	condensed chromosome
P	0000805	cellular_component	X chromosome
P	0000806	cellular_component	Y chromosome
P	0004672	molecular_function	protein kinase activity
P	0004674	molecular_function	protein serine/threonine kinase activity
P	0004693	molecular_function	cyclin-dependent protein serine/threonine kinase activity
P	0005515	molecular_function	protein binding
P	0005524	molecular_function	ATP binding
P	0005634	cellular_component	nucleus
P	0005635	cellular_component	nuclear envelope
P	0005654	cellular_component	nucleoplasm
P	0005667	cellular_component	transcription regulator complex
P	0005737	cellular_component	cytoplasm
P	0005768	cellular_component	endosome
P	0005813	cellular_component	centrosome
P	0005829	cellular_component	cytosol
P	0006260	biological_process	DNA replication
P	0006281	biological_process	DNA repair
P	0006338	biological_process	chromatin remodeling
P	0006468	biological_process	protein phosphorylation
P	0006974	biological_process	DNA damage response
P	0007099	biological_process	centriole replication
P	0007165	biological_process	signal transduction
P	0007265	biological_process	Ras protein signal transduction
P	0007346	biological_process	regulation of mitotic cell cycle
P	0008284	biological_process	positive regulation of cell population proliferation
P	0015030	cellular_component	Cajal body
P	0016301	molecular_function	kinase activity
P	0016740	molecular_function	transferase activity
P	0018105	biological_process	peptidyl-serine phosphorylation
P	0019904	molecular_function	protein domain specific binding
P	0030332	molecular_function	cyclin binding
P	0031453	biological_process	positive regulation of heterochromatin formation
P	0031571	biological_process	mitotic G1 DNA damage checkpoint signaling
P	0035173	molecular_function	histone kinase activity
P	0036064	cellular_component	ciliary basal body
P	0043247	biological_process	telomere maintenance in response to DNA damage
P	0043687	biological_process	post-translational protein modification
P	0045740	biological_process	positive regulation of DNA replication
P	0046872	molecular_function	metal ion binding
P	0051298	biological_process	centrosome duplication
P	0051301	biological_process	cell division
P	0051321	biological_process	meiotic cell cycle
P	0071732	biological_process	cellular response to nitric oxide
P	0090398	biological_process	cellular senescence
P	0097123	cellular_component	cyclin A1-CDK2 complex
P	0097124	cellular_component	cyclin A2-CDK2 complex
P	0097134	cellular_component	cyclin E1-CDK2 complex
P	0097135	cellular_component	cyclin E2-CDK2 complex
P	0097472	molecular_function	cyclin-dependent protein kinase activity
P	0106310	molecular_function	protein serine kinase activity
P	0120186	biological_process	negative regulation of protein localization to chromatin
P	0120261	biological_process	regulation of heterochromatin organization
P	1905784	biological_process	regulation of anaphase-promoting complex-dependent catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 89E P 301

Chain	Residue
P	ILE10
P	ASP145
P	HOH556
P	ALA31
P	PHE80
P	GLU81
P	PHE82
P	LEU83
P	HIS84
P	GLN85
P	LEU134

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
P	ILE10-LYS33

---

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

Chain	Residue	Details
P	VAL123-ILE135

---

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	15
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Site: {"description":"CDK7 binding","evidences":[{"source":"PubMed","id":"17373709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","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

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by WEE1","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
P	GLN131
P	ASP127

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
P	ASP127
P	LYS129

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
P	ASP127
P	LYS129
P	THR165

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
P	ASP127
P	LYS129
P	ASN132

---