Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1W0X

Crystal structure of human CDK2 in complex with the inhibitor olomoucine.

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000082	biological_process	G1/S transition of mitotic cell cycle
C	0000086	biological_process	G2/M transition of mitotic cell cycle
C	0000122	biological_process	negative regulation of transcription by RNA polymerase II
C	0000287	molecular_function	magnesium ion binding
C	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
C	0000781	cellular_component	chromosome, telomeric region
C	0000793	cellular_component	condensed chromosome
C	0000805	cellular_component	X chromosome
C	0000806	cellular_component	Y chromosome
C	0001673	cellular_component	male germ cell nucleus
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004693	molecular_function	cyclin-dependent protein serine/threonine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005635	cellular_component	nuclear envelope
C	0005654	cellular_component	nucleoplasm
C	0005667	cellular_component	transcription regulator complex
C	0005737	cellular_component	cytoplasm
C	0005768	cellular_component	endosome
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0006260	biological_process	DNA replication
C	0006281	biological_process	DNA repair
C	0006338	biological_process	chromatin remodeling
C	0006351	biological_process	DNA-templated transcription
C	0006468	biological_process	protein phosphorylation
C	0006813	biological_process	potassium ion transport
C	0007099	biological_process	centriole replication
C	0007165	biological_process	signal transduction
C	0007265	biological_process	Ras protein signal transduction
C	0007346	biological_process	regulation of mitotic cell cycle
C	0008284	biological_process	positive regulation of cell population proliferation
C	0010389	biological_process	regulation of G2/M transition of mitotic cell cycle
C	0010468	biological_process	regulation of gene expression
C	0015030	cellular_component	Cajal body
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
C	0018105	biological_process	peptidyl-serine phosphorylation
C	0019904	molecular_function	protein domain specific binding
C	0030332	molecular_function	cyclin binding
C	0031453	biological_process	positive regulation of heterochromatin formation
C	0031571	biological_process	mitotic G1 DNA damage checkpoint signaling
C	0032298	biological_process	positive regulation of DNA-templated DNA replication initiation
C	0035173	molecular_function	histone kinase activity
C	0043247	biological_process	telomere maintenance in response to DNA damage
C	0043687	biological_process	post-translational protein modification
C	0045740	biological_process	positive regulation of DNA replication
C	0045893	biological_process	positive regulation of DNA-templated transcription
C	0046872	molecular_function	metal ion binding
C	0051298	biological_process	centrosome duplication
C	0051301	biological_process	cell division
C	0051321	biological_process	meiotic cell cycle
C	0071732	biological_process	cellular response to nitric oxide
C	0090398	biological_process	cellular senescence
C	0097123	cellular_component	cyclin A1-CDK2 complex
C	0097124	cellular_component	cyclin A2-CDK2 complex
C	0097134	cellular_component	cyclin E1-CDK2 complex
C	0097135	cellular_component	cyclin E2-CDK2 complex
C	0097472	molecular_function	cyclin-dependent protein kinase activity
C	0106310	molecular_function	protein serine kinase activity
C	1905784	biological_process	regulation of anaphase-promoting complex-dependent catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLO C 1299

Chain	Residue
C	ILE10
C	ALA31
C	GLU81
C	PHE82
C	LEU83
C	ASP86
C	GLN131
C	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
C	ILE10-LYS33

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

Chain	Residue	Details
C	VAL123-ILE135

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
C	ASP127

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000269\|PubMed:17095507, ECO:0000269\|PubMed:21565702

Chain	Residue	Details
C	ILE10
C	LYS33
C	GLU81
C	ASP86
C	LYS129

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:21565702

Chain	Residue	Details
C	ASN132
C	ASP145

site_id	SWS_FT_FI4
Number of Residues	3
Details	SITE: CDK7 binding => ECO:0000269\|PubMed:17373709

Chain	Residue	Details
C	LYS9
C	LYS88
C	LEU166

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
C	MET1

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
C	LYS6

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:1396589, ECO:0000269\|PubMed:17095507

Chain	Residue	Details
C	THR14

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by WEE1 => ECO:0000269\|PubMed:1396589, ECO:0000269\|PubMed:17095507, ECO:0007744\|PubMed:19690332

Chain	Residue	Details
C	TYR15

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
C	TYR19

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CAK and CCRK => ECO:0000269\|PubMed:1396589, ECO:0000269\|PubMed:14597612, ECO:0000269\|PubMed:16325401, ECO:0000269\|PubMed:17095507, ECO:0000269\|PubMed:17570665, ECO:0000269\|PubMed:20147522, ECO:0000269\|PubMed:20360007, ECO:0000269\|PubMed:21565702, ECO:0000305\|PubMed:28666995

Chain	Residue	Details
C	THR160

Catalytic Information from CSA

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

Chain	Residue	Details
C	GLN131
C	ASP127

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

Chain	Residue	Details
C	ASP127
C	LYS129

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

Chain	Residue	Details
C	ASP127
C	LYS129
C	THR165

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

Chain	Residue	Details
C	ASP127
C	LYS129
C	ASN132

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)