6NPZ

Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate

Replaces:  6C0I

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	5
Details	binding site for residue MN A 501

Chain	Residue
A	GLU314
A	HIS354
A	HOH706
A	HOH749
B	HOH630

---

site_id	AC2
Number of Residues	2
Details	binding site for residue PGE A 502

Chain	Residue
A	GLN414
A	TYR417

---

site_id	AC3
Number of Residues	7
Details	binding site for residue PGE A 503

Chain	Residue
A	TYR350
A	LEU360
A	HOH639
A	HOH721
F	ARG2
A	LEU347
A	PHE349

---

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL B 501

Chain	Residue
B	LYS385
B	LYS386
B	ASP387
B	GLN390
B	HOH661
B	HOH719

---

site_id	AC5
Number of Residues	4
Details	binding site for residue VO4 B 502

Chain	Residue
A	ASN351
A	GLN352
B	HOH608
B	HOH739

---

site_id	AC6
Number of Residues	6
Details	binding site for residue MN B 503

Chain	Residue
B	GLU314
B	HIS354
B	HOH665
B	HOH709
B	HOH722
B	HOH731

---

site_id	AC7
Number of Residues	4
Details	binding site for residue MN F 101

Chain	Residue
A	ASP292
A	HOH631
F	ZXW7
F	HOH202

---

site_id	AC8
Number of Residues	4
Details	binding site for residue MN G 501

Chain	Residue
B	ASN279
B	ASP292
G	ZXW7
G	HOH606

---

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	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP274
B	ASP274

---

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

Chain	Residue	Details
A	LEU156
A	LYS179
B	LEU156
B	LYS179

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by caspase-3 => ECO:0000250|UniProtKB:P31750

Chain	Residue	Details
A	ASP462
B	ASP462

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER124
B	SER124

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER126
B	SER126

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER129
B	SER129

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by TNK2 => ECO:0000269|PubMed:20333297

Chain	Residue	Details
A	TYR176
B	TYR176

---

site_id	SWS_FT_FI8
Number of Residues	2
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
B	TPO308

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR448
A	THR450
B	THR448
B	THR450

---

site_id	SWS_FT_FI10
Number of Residues	2
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	SEP473
B	SEP473

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12149249

Chain	Residue	Details
A	TYR474
B	TYR474

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000269|PubMed:22629392

Chain	Residue	Details
A	SER126
A	SER129
B	SER126
B	SER129

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	CARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:22629392

Chain	Residue	Details
A	THR305
A	THR312
B	THR305
B	THR312

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250|UniProtKB:P31750

Chain	Residue	Details
A	SEP473
B	SEP473

---

site_id	SWS_FT_FI15
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22410793

Chain	Residue	Details
A	LYS284
B	LYS284

---