1HOD: Alpha-2A adrenergic receptor

NMR structure of D130I mutant T3-I2, a 32 residue peptide from the alpha 2A adrenergic receptor. Determined by solution NMR. Released 24 Jul 2002.

Method
Solution NMR
Chains
1
Atoms
266
Mol. weight
3.8 kDa
Released
24 Jul 2002

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

Secondary structure: helices and β-sheets

1HOD contains 2 α-helices and 0 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2-1312
α-helix20-267

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-2A adrenergic receptorAprotein32P08913 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HOD_1 ALPHA-2A ADRENERGIC RECEPTOR (chains A)
TSSIVHLCAISLIRYWSITQAIEYNLKRTPRR

Primary citation

NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix. Chung, D.A., Zuiderweg, E.R., Fowler, C.B. et al. Biochemistry (2002) 41:3596-3604. DOI 10.1021/bi015811+ · PubMed

Other PDB entries of the same protein (UniProt P08913 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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