1O6L

Crystal structure of an activated Akt/protein kinase B (PKB-PIF chimera) ternary complex with AMP-PNP and GSK3 peptide

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	4
Details	BINDING SITE FOR RESIDUE MN A1481

Chain	Residue
A	ASN280
A	ASP293
A	ANP1480
A	HOH2399

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A1482

Chain	Residue
A	ASP293
A	ANP1480
A	HOH2400
A	HOH2401

---

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ANP A1480

Chain	Residue
A	VAL166
A	ALA179
A	LYS181
A	THR213
A	MET229
A	GLU230
A	ALA232
A	GLU236
A	LYS277
A	GLU279
A	ASN280
A	MET282
A	THR292
A	ASP293
A	PHE439
A	MN1481
A	MN1482
A	HOH2011
A	HOH2016
A	HOH2393
A	HOH2394
A	HOH2395
A	HOH2396
A	HOH2397
A	HOH2398
A	HOH2399
C	ARG6
C	SER9
A	GLY159

---

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	1
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

---

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

Chain	Residue	Details
A	LEU158
A	LYS181

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12434148

Chain	Residue	Details
A	ASN280
A	ASP293

---

site_id	SWS_FT_FI4
Number of Residues	1
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

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER447

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR451

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	ASP474

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000250

Chain	Residue	Details
A	THR306
A	THR313

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU279
A	ASP275

---

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

Chain	Residue	Details
A	LYS277
A	ASP275

---

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

Chain	Residue	Details
A	THR313
A	LYS277
A	ASP275

---

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

Chain	Residue	Details
A	ASN280
A	LYS277
A	ASP275

---