3A8X

Crystal Structure of PKCiota kinase domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007163	biological_process	establishment or maintenance of cell polarity
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007163	biological_process	establishment or maintenance of cell polarity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 601

Chain	Residue
A	ARG337
A	GLN338
A	PRO473
A	ARG474
A	HOH782

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	GLY539
A	LEU540
A	ARG249
A	GLY536
A	GLU537
A	PHE538

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 604

Chain	Residue
A	ARG337
A	ILE446
A	LYS468
A	ARG471
A	HOH906

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 603

Chain	Residue
B	THR315
B	GLU316
B	HOH745

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK

Chain	Residue	Details
A	ILE251-LYS278

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

Chain	Residue	Details
A	ILE365-LEU377

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP369
B	ASP369

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE251
A	LYS274
B	ILE251
B	LYS274

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277, ECO:0000269|PubMed:11891849

Chain	Residue	Details
A	TYR256
B	TYR256

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277

Chain	Residue	Details
A	TYR271
A	TYR325
B	TYR271
B	TYR325

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:16125198

Chain	Residue	Details
A	TPO403
B	TPO403

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16125198, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TPO555
B	TPO555

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
A	ASP369	proton shuttle (general acid/base)
A	LYS371	electrostatic stabiliser
A	ASN374	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
B	ASP369	proton shuttle (general acid/base)
B	LYS371	electrostatic stabiliser
B	ASN374	electrostatic stabiliser

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