Structure of PDB 6npz Chain B Binding Site BS02
Receptor Information
>6npz Chain B (length=323) Species:
9606
(Homo sapiens) [
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PKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD
EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKI
TDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY
EMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQ
RLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDE
EFTAQMITIERRPHFPQFSYSAS
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
6npz Chain B Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
6npz
Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
Resolution
2.12 Å
Binding residue
(original residue number in PDB)
E314 H354
Binding residue
(residue number reindexed from 1)
E174 H214
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D274 K276 N279 D292 T312
Catalytic site (residue number reindexed from 1)
D134 K136 N139 D152 T172
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
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:6npz
,
PDBe:6npz
,
PDBj:6npz
PDBsum
6npz
PubMed
30078705
UniProt
P31749
|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)
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