Structure of PDB 6buu Chain A Binding Site BS01
Receptor Information
>6buu Chain A (length=323) Species:
9606
(Homo sapiens) [
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RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMITITSERRPHFPQFSYSASG
Ligand information
>6buu Chain F (length=10) Species:
9606
(Homo sapiens) [
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GRPRTTaFAE
Receptor-Ligand Complex Structure
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PDB
6buu
Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
G159 T160 V164 A177 K179 H194 A230 E234 F236 D274 K276 E278 M281 F309 C310 G311 T312 E314 Y315 E341 L347 F438
Binding residue
(residue number reindexed from 1)
G16 T17 V21 A34 K36 H51 A87 E91 F93 D131 K133 E135 M138 F166 C167 G168 T169 E171 Y172 E198 L204 F295
Enzymatic activity
Catalytic site (original residue number in PDB)
D274 K276 N279 D292 T312
Catalytic site (residue number reindexed from 1)
D131 K133 N136 D149 T169
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
View graph for
Biological Process
External links
PDB
RCSB:6buu
,
PDBe:6buu
,
PDBj:6buu
PDBsum
6buu
PubMed
30078705
UniProt
P31749
|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)
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