1GZK: Rac-beta serine/threonine protein kinase

Name: PDB 1GZK: Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
Published: 2003-05-22
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: kinase

Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 May 2003.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 2,481
Mol. weight: 36.49 kDa
Released: 22 May 2003

Explore 1GZK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GZK contains 14 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	149-151	3
β-strand	152-160	9	1
β-strand	164-171	8	1
β-strand	176-184	9	1
α-helix	203-206	4
β-strand	209	1	2
β-strand	212	1	2
β-strand	215-220	6	1
β-strand	224-230	7	1
β-strand	236	1	2
α-helix	237-242	6
α-helix	249-268	20
α-helix	278-280	3
β-strand	281-283	3	2
β-strand	289-291	3	2
α-helix	319-324	6
α-helix	330-345	16
α-helix	358-364	7
α-helix	365-367	3
α-helix	375-384	10
α-helix	389-391	3
α-helix	400-404	5
α-helix	414-419	6
α-helix	423-424	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rac-beta serine/threonine protein kinase	A	protein	315	HOMO SAPIENS	P31751 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GZK_1 RAC-BETA SERINE/THREONINE PROTEIN KINASE (chains A)
KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQ
NTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY
LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDN
DYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL
KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTA
QSITITPPDRYDSLG

Primary citation

Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation. Yang, J., Cron, P., Thompson, V. et al. Mol Cell (2002) 9:1227. DOI 10.1016/S1097-2765(02)00550-6 · PubMed

Other PDB entries of the same protein (UniProt P31751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1O6L 1.6 Å, Crystal structure of an activated Akt/protein kinase B (PKB-PIF chimera) ternary complex…
1O6K 1.7 Å, Structure of activated form of PKB kinase domain S474D with GSK3 peptide and AMP-PNP
2JDO 1.8 Å, Structure of pkb-beta (AKT2) complexed with isoquinoline-5-sulfonic acid…
2X39 1.93 Å, Structure of 4-Amino-N-(4-chlorobenzyl)-1-(7H-pyrrolo(2,3-d)pyrimidin-…
3D0E 2.0 Å, Crystal structure of human Akt2 in complex with GSK690693
9C1W 2.0 Å, Structure of AKT2 with compound 3
2UW9 2.1 Å, STRUCTURE OF PKB-BETA (AKT2) COMPLEXED WITH 4-(4-chloro-phenyl)-4-(4-(1H-pyrazol-4-yl)-ph…
2JDR 2.3 Å, Structure of pkb-beta (AKT2) complexed with the inhibitor a-443654
3E87 2.3 Å, Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors
8Q61 2.32 Å, Co-crystal structure of human AKT2 with compound 3
1GZN 2.5 Å, Structure of PKB kinase domain
3E88 2.5 Å, Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors

Browse structure collections

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