3E88

Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE G96 A 1

Chain	Residue
A	GLY159
A	PHE227
A	MET229
A	GLU230
A	TYR231
A	ALA232
A	MET282
A	THR292
A	ASP293
A	PHE294
A	PHE439
A	GLY161
A	GLY164
A	LYS165
A	VAL166
A	ALA179
A	LYS181
A	LEU183
A	GLU200

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE G96 B 1

Chain	Residue
B	GLY159
B	GLY164
B	LYS165
B	VAL166
B	ALA179
B	LYS181
B	LEU183
B	GLU200
B	MET229
B	GLU230
B	TYR231
B	ALA232
B	MET282
B	THR292
B	ASP293
B	PHE294
B	PHE439
D	SER9

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU158-LYS191

---

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

Chain	Residue	Details
A	VAL271-LEU283

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 => ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:35606353, ECO:0000269|PubMed:8250835

Chain	Residue	Details
C	SER9
D	SER9

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU158
A	LYS181
B	LEU158
B	LYS181

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12434148

Chain	Residue	Details
A	ASN280
A	ASP293
B	ASN280
B	ASP293

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493

Chain	Residue	Details
A	TPO309
B	TPO309

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER447
A	SER478
B	SER447
B	SER478

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TPO451
B	TPO451

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	ASP474
B	ASP474

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250

Chain	Residue	Details
A	THR306
A	THR313
B	THR306
B	THR313

---