1H10: Rac-alpha serine/threonine kinase

High resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to INS(1,3,4,5)-tetrakisphophate. Determined by X-ray diffraction at 1.4 Å resolution. Released 27 Jun 2003.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
1,266
Mol. weight
15.44 kDa
Ligands
4IP
Released
27 Jun 2003

Explore 1H10 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1H10 contains 3 α-helices and 7 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: 3 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix2-43
β-strand6-15101
β-strand22-3091
β-strand34-3851
α-helix45-484
β-strand53-5641
β-strand61-6551
β-strand72-7981
β-strand82-8981
α-helix93-11523

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rac-alpha serine/threonine kinaseAprotein125HOMO SAPIENSP31749 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1H10_1 RAC-ALPHA SERINE/THREONINE KINASE (chains A)
XSMSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVA
QCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEM
DFRSG

Ligands and cofactors

IDNameFormulaCopies
4IPInositol-(1,3,4,5)-tetrakisphosphateC6 H16 O18 P41

Primary citation

High Resolution Structure of the Pleckstrin Homology Domain of Protein Kinase B/Akt Bound to Phosphatidylinositol (3,4,5)-Trisphosphate. Thomas, C.C., Deak, M., Alessi, D.R. et al. Curr Biol (2002) 12:1256. DOI 10.1016/S0960-9822(02)00972-7 · PubMed

Other PDB entries of the same protein (UniProt P31749 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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