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THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 743

Chain	Residue
A	LYS154
A	ASP155
A	PHE232
A	HIS234
A	LYS235
A	HOH774
A	HOH799
A	HOH819
A	HOH935

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 744

Chain	Residue
A	TYR632
A	ARG635
A	ARG692
A	HOH854

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 745

Chain	Residue
A	GLY167
A	HIS168
A	PHE169
A	SER170
A	SO4747
A	HOH766

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 746

Chain	Residue
A	HIS145
A	PRO146
A	ALA147
A	LYS163
A	THR171
A	TRP173
A	HOH862
A	HOH918
A	HOH926

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 747

Chain	Residue
A	SER170
A	LYS187
A	ALA199
A	SO4745
A	HOH882

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 748

Chain	Residue
A	ARG568
A	ARG571

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 749

Chain	Residue
A	HIS262
A	GLU596
A	GLY600
A	PHE602
A	HOH925

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 750

Chain	Residue
A	GLU247
A	VAL248
A	LEU249
A	GLY250
A	LEU301

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU164-LYS187

---

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

Chain	Residue	Details
A	ILE290-MET302

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP294

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU164
A	LYS187

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	ASP615

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	HIS618

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	ALA620
A	THR642
A	TRP659

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	LEU625
A	ASP681
A	PRO685

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	VAL664
A	LYS677

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU298
A	ASP294

---

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

Chain	Residue	Details
A	ASP294
A	LYS296

---

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

Chain	Residue	Details
A	THR567
A	ASP294
A	LYS296

---

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

Chain	Residue	Details
A	ASP294
A	LYS296
A	ASN299

---