Structure of PDB 1o6k Chain A Binding Site BS03
Receptor Information
>1o6k Chain A (length=318) Species:
9606
(Homo sapiens) [
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KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVA
HTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRER
VFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFG
LCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGG
GPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITQRTHFPQFDYSASI
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1o6k Chain A Residue 1481 [
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Receptor-Ligand Complex Structure
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PDB
1o6k
Crystal Structure of an Activated Akt/Protein Kinase B Ternary Complex with Gsk-3 Peptide and AMP-Pnp
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
N280 D293
Binding residue
(residue number reindexed from 1)
N135 D148
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D275 K277 N280 D293 T313
Catalytic site (residue number reindexed from 1)
D130 K132 N135 D148 T168
Enzyme Commision number
2.7.11.1
: non-specific serine/threonine protein kinase.
Gene Ontology
Molecular Function
GO:0004672
protein kinase activity
GO:0004674
protein serine/threonine kinase activity
GO:0005524
ATP binding
Biological Process
GO:0006468
protein phosphorylation
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Molecular Function
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Biological Process
External links
PDB
RCSB:1o6k
,
PDBe:1o6k
,
PDBj:1o6k
PDBsum
1o6k
PubMed
12434148
UniProt
P31751
|AKT2_HUMAN RAC-beta serine/threonine-protein kinase (Gene Name=AKT2)
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