Structure of PDB 6npz Chain B

Receptor sequence
>6npzB (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
PKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKD
EVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKI
TDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMY
EMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQ
RLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDE
EFTAQMITIERRPHFPQFSYSAS
3D structure
PDB6npz Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
ChainB
Resolution2.12 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) D134 K136 N139 D152 T172
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 B G159 V164 A177 A230 E234 F236 D274 K276 E278 M281 D292 F309 C310 G311 T312 P313 E314 Y315 E341 F438 G19 V24 A37 A90 E94 F96 D134 K136 E138 M141 D152 F169 C170 G171 T172 P173 E174 Y175 E201 F298
BS02 MN B E314 H354 E174 H214
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:6npz, PDBe:6npz, PDBj:6npz
PDBsum6npz
PubMed30078705
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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