4RA5

Human Protein Kinase C THETA IN COMPLEX WITH LIGAND COMPOUND 11a (6-[(1,3-Dimethyl-azetidin-3-yl)-methyl-amino]-4(R)-methyl-7-phenyl-2,10-dihydro-9-oxa-1,2,4a-triaza-phenanthren-3-one)

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	0004697	molecular_function	diacylglycerol-dependent serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004697	molecular_function	diacylglycerol-dependent serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 3L0 A 801

Chain	Residue
A	LEU386
A	LEU511
A	ASP522
A	PHE664
A	GLY387
A	LYS388
A	VAL394
A	ALA407
A	MET458
A	GLU459
A	LEU461
A	ASP508

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 802

Chain	Residue
A	ASP594
A	HOH915
A	HOH916

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 803

Chain	Residue
A	ASP504
A	LYS506
A	ASP508
A	ASP522

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 804

Chain	Residue
A	GLY389
A	SER390

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site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 3L0 B 801

Chain	Residue
B	LEU386
B	LYS388
B	THR442
B	MET458
B	GLU459
B	LEU461
B	ASP465
B	ASP508
B	ASP522

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU386-LYS409

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

Chain	Residue	Details
A	ILE500-LEU512

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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	ASP504
B	ASP504

---

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

Chain	Residue	Details
A	LEU386
B	LEU386

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS409
B	LYS409

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:11772397, ECO:0000305|PubMed:15364937, ECO:0000305|PubMed:16252004

Chain	Residue	Details
A	GLU538
B	GLU538

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:16252004, ECO:0000269|Ref.37, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SEP676
B	SEP676

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER685
B	SER685

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:15364937, ECO:0000269|PubMed:16252004, ECO:0000269|Ref.37, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SEP695
B	SEP695

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