2IZX: PDB entry 2IZX

Molecular Basis of AKAP Specificity for PKA Regulatory Subunits. Determined by X-ray diffraction at 1.3 Å resolution. Released 8 Nov 2006.

Method
X-ray diffraction
Resolution
1.3 Å
Organisms
HOMO SAPIENS, SYNTHETIC CONSTRUCT
Chains
3
Atoms
915
Mol. weight
11.96 kDa
Ligands
DTD
Released
8 Nov 2006

Explore 2IZX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IZX contains 5 α-helices and 0 β-strands across 3 chains. 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4215
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix9-2315
α-helix28-4114
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix5-2016

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Camp-dependent protein kinase type II-alpha regulatory subunitA, Bprotein41HOMO SAPIENSP13861 (AlphaFold model)
Akap-isCprotein18SYNTHETIC CONSTRUCT
Sequence of entity 1 (A, B), FASTA
>2IZX_1 CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY SUBUNIT (chains A, B)
IQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREAR
Sequence of entity 2 (C), FASTA
>2IZX_2 AKAP-IS (chains C)
QIEYLAKQIVDNAIQQAK

Ligands and cofactors

IDNameFormulaCopies
DTDDithiane diolC4 H8 O2 S22

Primary citation

Molecular Basis of Akap Specificity for Pka Regulatory Subunits. Gold, M.G., Lygren, B., Dokurno, P. et al. Mol Cell (2006) 24:383. DOI 10.1016/J.MOLCEL.2006.09.006 · PubMed

Other PDB entries of the same protein (UniProt P13861 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2IZX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.