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BioLiP

Structure of PDB 6buu Chain B Binding Site BS01

Receptor Information
>6buu Chain B (length=319) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMITERRPHFPQFSYSAS
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6buu Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		T160 V164 A177 H194 A230 E234 F236 D274 K276 E278 M281 F309 C310 G311 T312 P313 E314 Y315 E341 F438
Binding residue
(residue number reindexed from 1)		T17 V21 A34 H51 A87 E91 F93 D131 K133 E135 M138 F166 C167 G168 T169 P170 E171 Y172 E198 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

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Molecular Function
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Biological Process
External links
PDB RCSB:6buu, PDBe:6buu, PDBj:6buu
PDBsum6buu
PubMed30078705
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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