6ILZ

Crystal structure of PKCiota in complex with inhibitor

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
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007163	biological_process	establishment or maintenance of cell polarity
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
E	0007163	biological_process	establishment or maintenance of cell polarity
G	0004672	molecular_function	protein kinase activity
G	0004674	molecular_function	protein serine/threonine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
G	0007163	biological_process	establishment or maintenance of cell polarity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue AFU A 601

Chain	Residue
A	ILE260
A	LYS283
A	GLU333
A	TYR334
A	VAL335
A	THR395
A	ASP396
A	PHE552
A	ASP553

---

site_id	AC2
Number of Residues	10
Details	binding site for residue AFU C 601

Chain	Residue
C	ILE260
C	VAL316
C	ILE332
C	GLU333
C	TYR334
C	VAL335
C	THR395
C	ASP396
C	PHE552
C	ASP553

---

site_id	AC3
Number of Residues	8
Details	binding site for residue AFU E 601

Chain	Residue
E	ILE260
E	ILE332
E	GLU333
E	TYR334
E	VAL335
E	LEU385
E	THR395
E	ASP396

---

site_id	AC4
Number of Residues	8
Details	binding site for residue AFU G 601

Chain	Residue
G	ILE260
G	VAL268
G	ILE332
G	GLU333
G	VAL335
G	THR395
G	ASP396
G	PHE552

---

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	ILE260-LYS287

---

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

Chain	Residue	Details
A	ILE374-LEU386

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP378
C	ASP378
E	ASP378
G	ASP378

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE260
A	LYS283
C	ILE260
C	LYS283
E	ILE260
E	LYS283
G	ILE260
G	LYS283

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277, ECO:0000269|PubMed:11891849

Chain	Residue	Details
A	TYR265
C	TYR265
E	TYR265
G	TYR265

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277

Chain	Residue	Details
A	TYR280
A	TYR334
C	TYR280
C	TYR334
E	TYR280
E	TYR334
G	TYR280
G	TYR334

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:16125198

Chain	Residue	Details
A	TPO412
C	TPO412
E	TPO412
G	TPO412

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16125198, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TPO564
C	TPO564
E	TPO564
G	TPO564

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
A	ASP378	proton shuttle (general acid/base)
A	LYS380	electrostatic stabiliser
A	ASN383	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
C	ASP378	proton shuttle (general acid/base)
C	LYS380	electrostatic stabiliser
C	ASN383	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
E	ASP378	proton shuttle (general acid/base)
E	LYS380	electrostatic stabiliser
E	ASN383	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
G	ASP378	proton shuttle (general acid/base)
G	LYS380	electrostatic stabiliser
G	ASN383	electrostatic stabiliser

---