3IW4

Crystal structure of PKC alpha in complex with NVP-AEB071

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LW4 A 901

Chain	Residue
A	LEU345
A	VAL420
A	ASP467
A	MET470
A	ALA480
A	ASP481
A	PHE350
A	VAL353
A	ALA366
A	GLU387
A	THR401
A	MET417
A	GLU418
A	TYR419

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LW4 B 901

Chain	Residue
B	LEU345
B	PHE350
B	ALA366
B	GLU387
B	THR401
B	MET417
B	GLU418
B	TYR419
B	VAL420
B	ASP424
B	ASP467
B	MET470
B	ALA480
B	ASP481

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE LW4 C 901

Chain	Residue
C	LEU345
C	PHE350
C	VAL353
C	ALA366
C	LYS368
C	GLU387
C	THR401
C	GLU418
C	TYR419
C	VAL420
C	ASP467
C	ASN468
C	MET470
C	ALA480
C	ASP481

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU345-LYS368

---

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

Chain	Residue	Details
A	ILE459-LEU471

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP463
B	ASP463
C	ASP463

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU345
A	LYS368
B	LEU345
B	LYS368
C	LEU345
C	LYS368

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04409

Chain	Residue	Details
A	THR494
A	THR495
B	THR494
B	THR495
C	THR494
C	THR495

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P04409, ECO:0000305

Chain	Residue	Details
A	GLU497
B	GLU497
C	GLU497

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P05771

Chain	Residue	Details
A	THR501
B	THR501
C	THR501

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS628
B	LYS628
C	LYS628

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P68403, ECO:0000255

Chain	Residue	Details
A	THR631
B	THR631
C	THR631

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TPO638
B	TPO638
C	TPO638

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976

Chain	Residue	Details
A	SER651
B	SER651
C	SER651

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SEP657
B	SEP657
C	SEP657

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by SYK => ECO:0000250|UniProtKB:P20444

Chain	Residue	Details
A	TYR658
B	TYR658
C	TYR658

---