Structure of PDB 6npz Chain A

Receptor sequence
>6npzA (length=322) Species: 9606 (Homo sapiens) [Search protein sequence]
KHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDE
VAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSR
ERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKIT
DFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYE
MMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQR
LGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEE
FTAQMITIRRPHFPQFSYSASG
3D structure
PDB6npz Akt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
ChainA
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) D133 K135 N138 D151 T171
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 G159 T160 V164 A177 H194 E234 F236 D274 K276 E278 M281 F309 C310 G311 T312 E314 F438 G18 T19 V23 A36 H53 E93 F95 D133 K135 E137 M140 F168 C169 G170 T171 E173 F297
BS02 MN A E314 H354 E173 H213
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:6npz, PDBe:6npz, PDBj:6npz
PDBsum6npz
PubMed30078705
UniProtP31749|AKT1_HUMAN RAC-alpha serine/threonine-protein kinase (Gene Name=AKT1)

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