5LI1

Structure of a Par3-inhibitory peptide bound to PKCiota core 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue ANP A 601

Chain	Residue
A	GLY261
A	GLU333
A	VAL335
A	ASP339
A	ASP382
A	ASN383
A	LEU385
A	ASP396
A	PHE552
A	MG604
A	HOH716
A	GLY263
A	HOH725
A	HOH733
A	HOH746
A	HOH774
A	SER264
A	TYR265
A	ALA266
A	VAL268
A	ALA281
A	LYS283
A	ILE332

---

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 602

Chain	Residue
A	THR301
A	ARG377
A	CYS400
A	LYS401
A	GLU402
A	TPO412
A	HOH702
A	HOH814

---

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

Chain	Residue
A	ALA309
A	HIS312
A	LEU315
A	GLU333
A	HOH815

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG A 604

Chain	Residue
A	ASN383
A	ASP396
A	ANP601
A	HOH774
A	HOH781

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG A 605

Chain	Residue
A	ASP292
A	GLU294
A	ASP295
B	LYS16
B	THR18
B	HOH113

---

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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP378

---

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

Chain	Residue	Details
A	ILE260
A	LYS283

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277, ECO:0000269|PubMed:11891849

Chain	Residue	Details
A	TYR265

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277

Chain	Residue	Details
A	TYR280
A	TYR334

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:16125198

Chain	Residue	Details
A	TPO412

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16125198, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	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

---