1UU3

Structure of human PDK1 kinase domain in complex with LY333531

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	7
Details	BINDING SITE FOR RESIDUE SO4 A1367

Chain	Residue
A	LYS76
A	ARG131
A	THR148
A	PHE149
A	GLN150
A	HOH2274
A	HOH2275

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A1368

Chain	Residue
A	SER160
A	GLN220
A	GOL1359
A	HOH2161
A	HOH2276
A	LYS144
A	TYR146

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A1369

Chain	Residue
A	ARG106
A	PRO140
A	LYS144
A	HIS351
A	GOL1359
A	SO41373
A	HOH2277
A	HOH2278
A	HOH2279

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A1370

Chain	Residue
A	LYS83
A	VAL345
A	THR346
A	TRP347
A	GLU348

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A1371

Chain	Residue
A	GLY91
A	SER92
A	PHE93
A	SER94
A	GOL1360
A	LY41374

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A1372

Chain	Residue
A	ARG75
A	ARG136
A	LYS199

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A1373

Chain	Residue
A	ARG106
A	GLU107
A	HIS351
A	GLN352
A	GOL1359
A	SO41369
A	HOH2042
A	HOH2281
A	HOH2282

---

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE LY4 A1374

Chain	Residue
A	LEU88
A	GLY89
A	ALA109
A	LYS111
A	GLU130
A	VAL143
A	LEU159
A	SER160
A	TYR161
A	ALA162
A	GLY165
A	GLU166
A	GLU209
A	ASN210
A	LEU212
A	THR222
A	ASP223
A	GOL1366
A	SO41371

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A1359

Chain	Residue
A	ARG106
A	GLU107
A	TYR108
A	TYR161
A	SO41368
A	SO41369
A	SO41373
A	HOH2104
A	HOH2278

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A1360

Chain	Residue
A	LYS111
A	LEU113
A	TYR126
A	VAL127
A	GLU130
A	SO41371

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A1361

Chain	Residue
A	PRO79
A	LYS154
A	TYR156
A	GLU328
A	GLU331
A	GLY332
A	HOH2268

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A1362

Chain	Residue
A	LYS76
A	PHE147
A	THR148
A	HOH2092

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A1363

Chain	Residue
A	LEU297
A	TYR299
A	PHE301

---

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A1364

Chain	Residue
A	TRP347
A	GLU348
A	ASN349
A	LEU350
A	HIS351
A	ALA103
A	THR104
A	SER105
A	HIS139
A	SER191

---

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A1365

Chain	Residue
A	PHE82
A	LYS83
A	PHE84
A	GLU194
A	GLY334
A	LYS337
A	HOH2269
A	HOH2270
A	HOH2273

---

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A1366

Chain	Residue
A	GLY89
A	GLU90
A	LY41374
A	HOH2021
A	HOH2109

---

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

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	GLU209
A	ASP205

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS207
A	ASP205

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS207
A	THR245
A	ASP205

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	LYS207
A	ASN210
A	ASP205

---