5Y86

Crystal structure of kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000242	cellular_component	pericentriolar material
A	0000287	molecular_function	magnesium ion binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
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	0005856	cellular_component	cytoskeleton
A	0006468	biological_process	protein phosphorylation
A	0010494	cellular_component	cytoplasmic stress granule
A	0016301	molecular_function	kinase activity
A	0016607	cellular_component	nuclear speck
A	0016740	molecular_function	transferase activity
A	0030218	biological_process	erythrocyte differentiation
A	0035063	biological_process	nuclear speck organization
A	0035617	biological_process	stress granule disassembly
A	0043066	biological_process	negative regulation of apoptotic process
A	0043518	biological_process	negative regulation of DNA damage response, signal transduction by p53 class mediator
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0080135	biological_process	regulation of cellular response to stress
A	0106310	molecular_function	protein serine kinase activity
A	1902751	biological_process	positive regulation of cell cycle G2/M phase transition
A	1903008	biological_process	organelle disassembly
A	1903432	biological_process	regulation of TORC1 signaling

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue HRM A 601

Chain	Residue
A	ALA236
A	HOH735
A	LYS238
A	PHE288
A	GLU289
A	LEU290
A	LEU291
A	LEU342
A	ILE354
A	ASP355

---

site_id	AC2
Number of Residues	6
Details	binding site for residue PO4 A 602

Chain	Residue
A	LYS151
A	GLY218
A	SER219
A	LYS337
A	HOH745
A	HOH897

---

site_id	AC3
Number of Residues	5
Details	binding site for residue PO4 A 603

Chain	Residue
A	ARG313
A	LYS314
A	LYS524
A	HOH702
A	HOH734

---

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 604

Chain	Residue
A	ARG178
A	LYS440
A	TYR441

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 605

Chain	Residue
A	LYS151
A	LYS159
A	PTR369
A	ARG376

---

site_id	AC6
Number of Residues	8
Details	binding site for residue EDO A 606

Chain	Residue
A	ILE448
A	PRO520
A	SER523
A	LYS524
A	SER525
A	HOH744
A	HOH755
A	HOH768

---

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 607

Chain	Residue
A	ARG208
A	PHE278
A	HOH922

---

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO A 608

Chain	Residue
A	SER308
A	VAL309
A	ARG461
A	HOH947

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 609

Chain	Residue
A	LEU343
A	HIS346
A	GLY347
A	ARG348

---

site_id	AD1
Number of Residues	2
Details	binding site for residue EDO A 610

Chain	Residue
A	ARG450
A	CYS452

---

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO A 611

Chain	Residue
A	TYR296
A	GLU297
A	LYS300
A	HOH707

---

site_id	AD3
Number of Residues	9
Details	binding site for residue GOL A 612

Chain	Residue
A	TYR157
A	GLY180
A	VAL181
A	ILE182
A	ASP413
A	GLU414
A	GLY415
A	HOH704
A	HOH927

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE215-LYS238

---

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

Chain	Residue	Details
A	ILE331-LEU343

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	Motif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"29973724","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29634919","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23415227","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29634919","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"29634919","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q922Y0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---