2JDO

STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY) ETHYLAMINO)ETHYL)AMIDE

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 I5S A1480

Chain	Residue
A	LYS160
A	TYR231
A	ALA232
A	GLU236
A	GLU279
A	ASN280
A	MET282
A	ASP293
A	EDO1481
A	HOH2309
A	HOH2310
A	GLY161
C	ARG6
A	GLY164
A	LYS165
A	VAL166
A	ALA179
A	LYS181
A	MET229
A	GLU230

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A1481

Chain	Residue
A	GLU200
A	MET229
A	ASP293
A	PHE294
A	I5S1480
A	HOH2310

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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

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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

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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|UniProtKB:P31749

Chain	Residue	Details
A	THR306
A	THR313

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750

Chain	Residue	Details
A	ASP474

---

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

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