4A07

Human PDK1 Kinase Domain in Complex with Allosteric Activator PS171 Bound to the PIF-Pocket

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 500

Chain	Residue
A	GLY89
A	GLU166
A	LEU212
A	ASP223
A	MG800
A	HOH2019
A	HOH2128
A	HOH2131
A	HOH2132
A	HOH2209
A	GLY91
A	SER92
A	SER94
A	VAL96
A	ALA109
A	LYS111
A	SER160
A	ALA162

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AZ7 A 600

Chain	Residue
A	LYS76
A	LYS115
A	ILE119
A	VAL124
A	ARG131
A	THR148
A	GLN150
A	LEU155
A	PHE157

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AZ7 A 700

Chain	Residue
A	LEU168
A	ARG172
A	PHE242
A	LEU253
A	LEU254
A	LYS257
A	GLN274
A	GLY278
A	PHE282
A	ARG283
A	PHE291

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 800

Chain	Residue
A	LYS111
A	ASP223
A	ATP500

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 860

Chain	Residue
A	ASP311

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 870

Chain	Residue
A	LEU350

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 890

Chain	Residue
A	LYS169
A	TYR170

---

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

Chain	Residue	Details
A	ASP205

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	SER92
A	LYS111
A	SER160
A	GLU166
A	ASP223

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:22999883

Chain	Residue	Details
A	GLU209

---

site_id	SWS_FT_FI4
Number of Residues	1
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

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0

Chain	Residue	Details
A	LYS304

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756

Chain	Residue	Details
A	THR354

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