3ORX

PDK1 mutant bound to allosteric disulfide fragment inhibitor 1F8

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
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
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
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
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
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
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
H	0004672	molecular_function	protein kinase activity
H	0004674	molecular_function	protein serine/threonine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 A 1

Chain	Residue
A	ARG131
A	CYS148
A	PHE149
A	GLN150
A	LEU155

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 2

Chain	Residue
A	GLU348
A	HOH412

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 B 1

Chain	Residue
B	PHE149
B	GLN150
B	LEU155
B	ARG131
B	CYS148

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 5

Chain	Residue
B	TRP347
B	GLU348
B	HOH1082

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 C 1

Chain	Residue
C	ARG131
C	CYS148
C	PHE149
C	GLN150
C	LEU155

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 6

Chain	Residue
C	TRP347
C	GLU348
C	HOH884
C	HOH1186

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 D 1

Chain	Residue
D	ARG131
D	CYS148
D	PHE149
D	GLN150
D	LEU155

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 360

Chain	Residue
D	TRP347
D	GLU348
D	HOH1237

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1F8 E 1

Chain	Residue
E	ARG131
E	CYS148
E	PHE149
E	GLN150
E	LEU155
F	ILE119

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 F 1

Chain	Residue
E	ILE119
F	ARG131
F	CYS148
F	PHE149
F	LEU155

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1F8 G 1

Chain	Residue
G	ARG131
G	CYS148
G	PHE149
G	LEU155
H	ILE119

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1F8 H 1

Chain	Residue
H	ARG131
H	CYS148
H	PHE149
H	LEU155

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU88-LYS111

---

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

Chain	Residue	Details
A	ILE201-LEU213

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP205
B	ASP205
C	ASP205
D	ASP205
E	ASP205
F	ASP205
G	ASP205
H	ASP205

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	SER92
B	ASP223
C	SER92
C	LYS111
C	SER160
C	GLU166
C	ASP223
D	SER92
D	LYS111
D	SER160
D	GLU166
A	LYS111
D	ASP223
E	SER92
E	LYS111
E	SER160
E	GLU166
E	ASP223
F	SER92
F	LYS111
F	SER160
F	GLU166
A	SER160
F	ASP223
G	SER92
G	LYS111
G	SER160
G	GLU166
G	ASP223
H	SER92
H	LYS111
H	SER160
H	GLU166
A	GLU166
H	ASP223
A	ASP223
B	SER92
B	LYS111
B	SER160
B	GLU166

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	GLU209
B	GLU209
C	GLU209
D	GLU209
E	GLU209
F	GLU209
G	GLU209
H	GLU209

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10455013, ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:15772071, ECO:0000269|PubMed:16780920, ECO:0000269|Ref.8

Chain	Residue	Details
A	SEP241
B	SEP241
C	SEP241
D	SEP241
E	SEP241
F	SEP241
G	SEP241
H	SEP241

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0

Chain	Residue	Details
A	LYS304
B	LYS304
C	LYS304
D	LYS304
E	LYS304
F	LYS304
G	LYS304
H	LYS304

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756

Chain	Residue	Details
A	THR354
B	THR354
C	THR354
D	THR354
E	THR354
F	THR354
G	THR354
H	THR354

---