2LG1: Human AKAP13 PH domain and stabilizing DH helix

Solution structure of the human AKAP13 PH domain and stabilizing DH helix. Determined by solution NMR. Released 3 Aug 2011.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,472
Mol. weight
21.06 kDa
Released
3 Aug 2011

Explore 2LG1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2LG1 contains 4 α-helices and 11 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: 4 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix25-306
α-helix31-4515
β-strand53-5421
β-strand60-6121
α-helix63-664
β-strand71-80102
β-strand86-9492
β-strand97-9932
β-strand102-10433
β-strand107-10933
β-strand119-12132
β-strand126-12832
β-strand136-14052
β-strand150-15342
α-helix157-17721

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
A-kinase anchor protein 13Aprotein185Homo sapiensQ12802 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LG1_1 A-kinase anchor protein 13 (chains A)
SMTKDNEVEQEDLAQSLSLVKDVIGAVDSKVASYEKKVRLNEIYTKTDSKSIMRMKSGQM
FAKEDLKRKKLVRDGSVFLKNAAGRLKEVQAVLLTDILVFLQEKDQKYIFASLDQKSTVI
SLKKLIVREVAHEEKGLFLISMGMTDPEMVEVHASSKEERNSWIQIIQDTINTLNRDEDE
GIPSE

Primary citation

Structural Insights into the Activation of the RhoA GTPase by the Lbc Oncoprotein. Lenoir, M., Sugawara, M., Kaur, J. et al. J Biol Chem (2014) 3:215-218. DOI 10.1074/jbc.M114.561787 · PubMed

Other PDB entries of the same protein (UniProt Q12802 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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