3QHR

Structure of a pCDK2/CyclinA transition-state mimic

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000082	biological_process	G1/S transition of mitotic cell cycle
A	0000086	biological_process	G2/M transition of mitotic cell cycle
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0000307	cellular_component	cyclin-dependent protein kinase holoenzyme complex
A	0000781	cellular_component	chromosome, telomeric region
A	0000793	cellular_component	condensed chromosome
A	0000805	cellular_component	X chromosome
A	0000806	cellular_component	Y chromosome
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	0005635	cellular_component	nuclear envelope
A	0005654	cellular_component	nucleoplasm
A	0005667	cellular_component	transcription regulator complex
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0006260	biological_process	DNA replication
A	0006281	biological_process	DNA repair
A	0006338	biological_process	chromatin remodeling
A	0006468	biological_process	protein phosphorylation
A	0006974	biological_process	DNA damage response
A	0007099	biological_process	centriole replication
A	0007165	biological_process	signal transduction
A	0007265	biological_process	Ras protein signal transduction
A	0007346	biological_process	regulation of mitotic cell cycle
A	0008284	biological_process	positive regulation of cell population proliferation
A	0015030	cellular_component	Cajal body
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0018105	biological_process	peptidyl-serine phosphorylation
A	0019904	molecular_function	protein domain specific binding
A	0030332	molecular_function	cyclin binding
A	0031453	biological_process	positive regulation of heterochromatin formation
A	0031571	biological_process	mitotic G1 DNA damage checkpoint signaling
A	0035173	molecular_function	histone kinase activity
A	0036064	cellular_component	ciliary basal body
A	0043247	biological_process	telomere maintenance in response to DNA damage
A	0043687	biological_process	post-translational protein modification
A	0045740	biological_process	positive regulation of DNA replication
A	0046872	molecular_function	metal ion binding
A	0051298	biological_process	centrosome duplication
A	0051301	biological_process	cell division
A	0051321	biological_process	meiotic cell cycle
A	0071732	biological_process	cellular response to nitric oxide
A	0090398	biological_process	cellular senescence
A	0097123	cellular_component	cyclin A1-CDK2 complex
A	0097124	cellular_component	cyclin A2-CDK2 complex
A	0097134	cellular_component	cyclin E1-CDK2 complex
A	0097135	cellular_component	cyclin E2-CDK2 complex
A	0097472	molecular_function	cyclin-dependent protein kinase activity
A	0106310	molecular_function	protein serine kinase activity
A	0120186	biological_process	negative regulation of protein localization to chromatin
A	0120261	biological_process	regulation of heterochromatin organization
A	1905784	biological_process	regulation of anaphase-promoting complex-dependent catabolic process
B	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity
B	0044772	biological_process	mitotic cell cycle phase transition
C	0000082	biological_process	G1/S transition of mitotic cell cycle
C	0000086	biological_process	G2/M transition of mitotic cell cycle
C	0000166	molecular_function	nucleotide binding
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	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	0006260	biological_process	DNA replication
C	0006281	biological_process	DNA repair
C	0006338	biological_process	chromatin remodeling
C	0006468	biological_process	protein phosphorylation
C	0006974	biological_process	DNA damage response
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	0015030	cellular_component	Cajal body
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
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	0035173	molecular_function	histone kinase activity
C	0036064	cellular_component	ciliary basal body
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	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	0120186	biological_process	negative regulation of protein localization to chromatin
C	0120261	biological_process	regulation of heterochromatin organization
C	1905784	biological_process	regulation of anaphase-promoting complex-dependent catabolic process
D	0016538	molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity
D	0044772	biological_process	mitotic cell cycle phase transition

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP A 297

Chain	Residue
A	ILE10
A	LEU83
A	ASP86
A	GLN131
A	ASN132
A	LEU134
A	ASP145
A	MG298
A	MG299
A	MGF300
A	HOH307
A	GLY11
A	HOH341
A	HOH574
A	GLY13
A	THR14
A	TYR15
A	GLY16
A	ALA31
A	LYS33
A	GLU81

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 298

Chain	Residue
A	TYR15
A	ASP145
A	ADP297
A	MGF300
A	HOH306
A	HOH333

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 299

Chain	Residue
A	ASN132
A	ASP145
A	ADP297
A	MGF300
A	HOH341

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MGF A 300

Chain	Residue
A	GLY13
A	THR14
A	TYR15
A	ASP127
A	LYS129
A	ASN132
A	ASP145
A	ADP297
A	MG298
A	MG299
A	HOH306
A	HOH333
A	HOH654
K	THR0

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 301

Chain	Residue
A	PRO130
A	GLN131
A	HOH360

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	LYS105
A	ASP256
A	ASP258
A	PRO284
A	GLN287
A	ASP288

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 303

Chain	Residue
A	THR158
A	TYR159
A	TPO160
A	HIS161
A	GLU162
A	HOH559
B	TYR271

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 304

Chain	Residue
A	GLY-1
A	PHE4
A	ASN23
A	GLU28
A	ASP68
A	GOL305
A	HOH448

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 305

Chain	Residue
A	GLY-1
A	ASP68
A	GOL304
D	LYS300

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
B	HIS233
B	ASN237
B	PRO309
B	THR310
B	VAL311
B	HOH452

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 3

Chain	Residue
B	TYR199
B	ARG202
B	GLN203
B	LEU243
B	SER244
B	SER247

---

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 6

Chain	Residue
B	HOH91
B	SER209
B	ALA212
B	ASP343
B	HIS404
B	GLN406
B	HOH441
B	HOH518

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 8

Chain	Residue
B	THR380
B	HOH459
B	HOH502

---

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 16

Chain	Residue
B	TYR286
B	GLN290
B	HOH476
B	HOH483
L	LYS6
B	GLY251
B	LYS252
B	THR285

---

site_id	BC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP C 297

Chain	Residue
C	ILE10
C	GLY11
C	GLY13
C	THR14
C	TYR15
C	GLY16
C	ALA31
C	LYS33
C	GLU81
C	LEU83
C	ASP86
C	LYS89
C	GLN131
C	ASN132
C	LEU134
C	ASP145
C	MG298
C	MG299
C	MGF300
C	HOH308
C	HOH352
C	HOH551
C	HOH560
C	HOH561

---

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 298

Chain	Residue
C	TYR15
C	ASP145
C	ADP297
C	MGF300
C	HOH304
C	HOH551

---

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 299

Chain	Residue
C	ASN132
C	ASP145
C	ADP297
C	MGF300
C	HOH352

---

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MGF C 300

Chain	Residue
C	GLY13
C	THR14
C	TYR15
C	ASP127
C	LYS129
C	ASN132
C	ASP145
C	ADP297
C	MG298
C	MG299
J	THR0
J	HOH655

---

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL C 301

Chain	Residue
C	PRO130
C	GLN131

---

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 302

Chain	Residue
C	LYS88
C	MET91
C	ASP92
C	GLU195
C	ARG199
C	ARG200
C	ALA201

---

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 303

Chain	Residue
C	LYS56
C	LEU66
C	VAL69
C	HOH627

---

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL D 2

Chain	Residue
D	GLN379
D	THR380

---

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 5

Chain	Residue
D	HIS233
D	ASN237
D	PRO309
D	THR310
D	VAL311
D	LEU341
D	HOH567

---

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 7

Chain	Residue
D	MET200
D	GLN203
D	ILE206
D	THR207
D	ASN208

---

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 13

Chain	Residue
D	LYS252
D	GLN290
M	LYS6

---

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 15

Chain	Residue
D	TYR199
D	ARG202
D	LEU243
D	SER244
D	MET246
D	SER247

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	ARG211-PHE242

---

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

Chain	Residue	Details
A	VAL123-ILE135

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	30
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	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"CDK7 binding","evidences":[{"source":"PubMed","id":"17373709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
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	2
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	2
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	2
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	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by CAK and CCRK","evidences":[{"source":"PubMed","id":"1396589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14597612","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17095507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17570665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21565702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28666995","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---