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	352
Details	Region: {"description":"PIF-pocket","evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
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	56
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	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22999883","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	7
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	8
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	8
Details	Modified residue: {"description":"Phosphothreonine; by MELK","evidences":[{"source":"PubMed","id":"22544756","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---