3A8W

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	22
Details	BINDING SITE FOR RESIDUE ATP A 601

Chain	Residue
A	ILE251
A	GLU324
A	VAL326
A	ASP387
A	PHE543
A	HOH706
A	HOH714
A	HOH732
A	HOH736
A	HOH738
A	HOH742
A	GLY252
A	HOH794
A	HOH804
A	HOH847
A	GLY254
A	SER255
A	TYR256
A	ALA257
A	VAL259
A	LYS274
A	ILE323

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP B 601

Chain	Residue
B	ILE251
B	GLY252
B	ARG253
B	GLY254
B	SER255
B	TYR256
B	ALA257
B	VAL259
B	LYS274
B	VAL307
B	ILE323
B	GLU324
B	VAL326
B	ASP387
B	PHE543
B	HOH703
B	HOH718
B	HOH728
B	HOH779
B	HOH835
B	HOH836

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 611

Chain	Residue
B	ARG337
B	GLN338
B	ARG441
B	PRO473
B	ARG474
B	HOH752

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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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11891849","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"11713277","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"16125198","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16125198","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

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

---