5ACK

Human PDK1 Kinase Domain in Complex with Allosteric Compound 7 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	21
Details	BINDING SITE FOR RESIDUE ATP A 500

Chain	Residue
A	GLY89
A	ALA162
A	GLU166
A	LEU212
A	NA900
A	NA902
A	HOH2020
A	HOH2022
A	HOH2189
A	HOH2190
A	HOH2330
A	GLU90
A	HOH2331
A	HOH2332
A	GLY91
A	SER92
A	SER94
A	VAL96
A	ALA109
A	SER160
A	TYR161

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SVQ A 600

Chain	Residue
A	LYS115
A	VAL127
A	ARG131
A	THR148
A	PHE149
A	GLN150
A	LEU155

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DTD A 700

Chain	Residue
A	PHE242
A	VAL243
A	GLY244
A	GLU287
A	PHE291
A	HOH2221

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DMS A 800

Chain	Residue
A	THR104
A	SER105
A	HIS139
A	PHE141
A	TRP347
A	ASN349
A	LEU350
A	HIS351
A	HOH2027

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 900

Chain	Residue
A	ASP223
A	ATP500
A	NA902
A	HOH2022

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 901

Chain	Residue
A	GLY244
A	THR245
A	HOH2220
A	HOH2221

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 902

Chain	Residue
A	ASN210
A	ASP223
A	ATP500
A	NA900
A	HOH2181

---

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	44
Details	Region: {"description":"PIF-pocket","evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12169624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15741170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"10455013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11481331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15772071","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16780920","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z2A0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by MELK","evidences":[{"source":"PubMed","id":"22544756","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---