4GV1

PKB alpha in complex with AZD5363

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	20
Details	BINDING SITE FOR RESIDUE 0XZ A 501

Chain	Residue
A	GLY157
A	MET227
A	GLU228
A	ALA230
A	GLU234
A	GLU278
A	MET281
A	ASP292
A	PHE438
A	GOL505
A	HOH642
A	LYS158
A	HOH726
A	GLY159
A	GLY162
A	LYS163
A	VAL164
A	ALA177
A	LYS179
A	LEU181

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	LYS154
A	ASP434
A	THR435
A	ARG436
A	HOH732
A	HOH939

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	LYS179
A	ILE186
A	GLU191
A	THR195
A	GLU198
A	ASP292
A	GLY294
A	HOH854
A	HOH855

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	PHE309
A	CYS310
A	GLY311
A	THR312
A	PRO313
A	LEU316
A	HOH967

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	GLY157
A	LYS158
A	GLU234
A	PHE236
A	PHE442
A	0XZ501
A	HOH638
A	HOH709
A	HOH852

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	34
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVkekatgryyamkilkkevIVAK

Chain	Residue	Details
A	LEU156-LYS189

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKleNLML

Chain	Residue	Details
A	VAL270-LEU282

---

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	ASP274

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU156
A	LYS179

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage; by caspase-3 => ECO:0000250|UniProtKB:P31750

Chain	Residue	Details
A	ASP462

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297

Chain	Residue	Details
A	TYR176

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by IKKE, PDPK1 and TBK1 => ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18456494, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9512493

Chain	Residue	Details
A	TPO308

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR448
A	THR450

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by IKKE, MTOR and TBK1; alternate => ECO:0000269|PubMed:14761976, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:17013611, ECO:0000269|PubMed:20333297, ECO:0000269|PubMed:20978158, ECO:0000269|PubMed:21464307, ECO:0000269|PubMed:23799035, ECO:0000269|PubMed:8978681, ECO:0000269|PubMed:9736715

Chain	Residue	Details
A	ASP473

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12149249

Chain	Residue	Details
A	TYR474

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392

Chain	Residue	Details
A	THR305
A	THR312

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750

Chain	Residue	Details
A	ASP473

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22410793

Chain	Residue	Details
A	LYS284

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