Structure of PDB 4ekk Chain A

Receptor sequence
>4ekkA (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
RVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVA
HTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRER
VFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDF
GLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM
CGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLG
GGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFT
AQMISERRPHFPQFDYSAS
3D structure
PDB4ekk An ATP-Site On-Off Switch That Restricts Phosphatase Accessibility of Akt.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A E234 F236 K276 L277 E278 T308 F309 C310 G311 T312 P313 E314 Y315 L316 E341 E91 F93 K133 L134 E135 T165 F166 C167 G168 T169 P170 E171 Y172 L173 E198
BS02 ANP A V164 A177 K179 E234 K276 M281 D292 F438 V21 A34 K36 E91 K133 M138 D149 F295
BS03 MN A N279 D292 N136 D149
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
View graph for
Biological Process
External links
PDB RCSB:4ekk, PDBe:4ekk, PDBj:4ekk
PDBsum4ekk
PubMed22569334
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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