Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T67619 Target Info
Target Name RAC-alpha serine/threonine-protein kinase (AKT1)
Synonyms RAC-PK-alpha; RAC; Proto-oncogene c-Akt; Protein kinase B alpha; PKB alpha
Target Type Successful Target
Gene Name AKT1
Biochemical Class Kinase
UniProt ID
AKT1_HUMAN
Ligand General Information  Top
Ligand Name Inositol 1,3,4,5-Tetrakisphosphate Ligand Info
Canonical SMILES C1(C(C(C(C(C1OP(=O)(O)O)OP(=O)(O)O)OP(=O)(O)O)O)OP(=O)(O)O)O
InChI 1S/C6H16O18P4/c7-1-3(21-25(9,10)11)2(8)5(23-27(15,16)17)6(24-28(18,19)20)4(1)22-26(12,13)14/h1-8H,(H2,9,10,11)(H2,12,13,14)(H2,15,16,17)(H2,18,19,20)/t1-,2-,3?,4-,5+,6?/m0/s1
InChIKey CIPFCGZLFXVXBG-FTSGZOCFSA-N
PubChem Compound ID 107758
Drug Binding Sites of Target  Top
PDB ID: 1UNQ      High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate
Method X-ray diffraction Resolution 0.98 Å Mutation No [1]
PDB Sequence
SMSDVAIVKE
9
GWLHKRGEYI
19
KTWRPRYFLL
29
KNDGTFIGYK
39
ERPQDVDQRE
49

APLNNFSVAQ
59
CQLMKTERPR
69
PNTFIIRCLQ
79
WTTVIERTFH
89
VETPEEREEW
99

TTAIQTVADG
109
LKKQEEEE
Residue
Distance (Å)
LYS14
2.693
ARG15
4.397
GLY16
3.657
GLU17
2.974
TYR18
2.848
ILE19
2.759
ARG23
2.796
Residue
Distance (Å)
ARG25
2.930
LEU52
3.649
ASN53
2.928
ASN54
4.770
PHE55
3.422
ARG86
2.800
PDB ID: 1H10      HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE
Method X-ray diffraction Resolution 1.40 Å Mutation No [2]
PDB Sequence
SSDVAIVKEG
10
WLHKRGEYIK
20
TWRPRYFLLK
30
NDGTFIGYKE
40
RPQDVDQREA
50

PLNNFSVAQC
60
QLKTERPRPN
71
TFIIRCLQWT
81
TVIERTFHVE
91
TPEEREEWTT
101

AIQTVADGLK
111
KQEEE
Residue
Distance (Å)
LYS14
2.694
ARG15
4.399
GLY16
3.644
GLU17
2.976
TYR18
2.853
ILE19
2.766
LYS20
4.993
Residue
Distance (Å)
ARG23
2.811
ARG25
2.939
LEU52
3.693
ASN53
2.629
ASN54
4.782
PHE55
3.492
ARG86
2.862
PDB ID: 2UZS      A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K)
Method X-ray diffraction Resolution 2.46 Å Mutation Yes [3]
PDB Sequence
SMSDVAIVKE
9
GWLHKRGKYI
19
KTWRPRYFLL
29
KNDGTFIGYK
39
ERPQDVDQRE
49

APLNNFSVAQ
59
CQLMKTERPR
69
PNTFIIRCLQ
79
WTTVIERTFH
89
VETPEEREEW
99

TTAIQTVADG
109
LKKQEEEE
Residue
Distance (Å)
LYS14
2.825
ARG15
4.120
GLY16
3.447
LYS17
3.102
TYR18
2.935
ILE19
2.872
ARG23
2.692
Residue
Distance (Å)
ARG25
2.859
LEU52
3.850
ASN53
2.969
ASN54
4.389
PHE55
4.392
ARG86
2.613
References  Top
REF 1 Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem J. 2003 Nov 1;375(Pt 3):531-8.
REF 2 High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate. Curr Biol. 2002 Jul 23;12(14):1256-62.
REF 3 A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Nature. 2007 Jul 26;448(7152):439-44.

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