3ORZ

PDK1 mutant bound to allosteric disulfide fragment activator 2A2

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 2A2 A 1

Chain	Residue
A	LYS115
A	ILE118
A	ILE119
A	ILE119
A	CYS148
A	PHE149
A	LEU155

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BI4 A 360

Chain	Residue
A	GLY91
A	ALA109
A	LYS111
A	VAL143
A	LEU159
A	SER160
A	TYR161
A	ALA162
A	GLU209
A	LEU212
A	THR222
A	ASP223
A	HOH393
A	LEU88
A	GLY89

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2A2 B 1

Chain	Residue
B	LYS115
B	ILE118
B	ILE119
B	ARG131
B	CYS148
B	PHE149
B	LEU155
D	2A21

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BI4 B 360

Chain	Residue
B	LEU88
B	GLY89
B	GLU90
B	GLY91
B	ALA109
B	LYS111
B	VAL143
B	LEU159
B	SER160
B	TYR161
B	ALA162
B	GLU209
B	LEU212
B	THR222
B	ASP223
B	HOH375

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 2A2 C 1

Chain	Residue
C	LYS115
C	ILE118
C	ILE119
C	CYS148
C	PHE149

---

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BI4 C 360

Chain	Residue
C	LEU88
C	GLY89
C	GLY91
C	ALA109
C	LYS111
C	VAL143
C	LEU159
C	SER160
C	TYR161
C	ALA162
C	GLU209
C	LEU212
C	THR222
C	ASP223
C	HOH373
C	HOH823

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2A2 D 1

Chain	Residue
B	2A21
D	LYS115
D	ILE118
D	VAL124
D	ARG131
D	CYS148
D	PHE149
D	LEU155

---

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BI4 D 360

Chain	Residue
D	LEU88
D	GLY89
D	GLY91
D	ALA109
D	LYS111
D	VAL143
D	LEU159
D	SER160
D	TYR161
D	ALA162
D	GLU209
D	LEU212
D	THR222
D	ASP223
D	HOH378

---

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	4
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

---

site_id	SWS_FT_FI2
Number of Residues	20
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
A	SER160
A	GLU166
A	ASP223
B	SER92
B	LYS111
B	SER160
B	GLU166

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	GLU209
B	GLU209
C	GLU209
D	GLU209

---

site_id	SWS_FT_FI4
Number of Residues	4
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

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0

Chain	Residue	Details
A	LYS304
B	LYS304
C	LYS304
D	LYS304

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756

Chain	Residue	Details
A	THR354
B	THR354
C	THR354
D	THR354

---