2VT4: BETA1 adrenergic receptor

Turkey BETA1 adrenergic receptor with stabilising mutations and bound cyanopindolol. Determined by X-ray diffraction at 2.7 Å resolution. Released 24 Jun 2008.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
MELEAGRIS GALLOPAVO
Chains
4
Atoms
8,976
Mol. weight
148.24 kDa
Ligands
D10, SOG, P32
Released
24 Jun 2008

Explore 2VT4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VT4 contains 63 α-helices and 8 β-strands across 4 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: 15 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix41-6828
α-helix70-723
α-helix75-8915
α-helix90-945
α-helix95-10410
α-helix111-14232
α-helix146-1527
α-helix155-17824
β-strand18311
α-helix187-1948
β-strand20311
α-helix205-2128
α-helix213-2175
α-helix218-23518
α-helix285-31531
α-helix322-34322
α-helix347-35610
Chain B: 17 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix40-6829
α-helix75-8915
α-helix90-945
α-helix95-10410
α-helix111-14434
α-helix146-1527
α-helix155-16915
α-helix170-1745
α-helix175-1784
β-strand18312
α-helix187-1948
β-strand20312
α-helix205-2128
α-helix213-2175
α-helix218-23518
α-helix285-31531
α-helix322-34221
α-helix343-3453
α-helix347-35610
Chain C: 16 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix40-6829
α-helix75-8915
α-helix90-945
α-helix95-10410
α-helix111-14434
α-helix146-1527
α-helix155-16915
α-helix170-1745
α-helix175-1784
β-strand18313
α-helix187-1948
β-strand20313
α-helix205-2128
α-helix213-2175
α-helix218-23518
α-helix285-31531
α-helix322-34221
α-helix343-3453
Chain D: 15 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix42-6827
α-helix70-723
α-helix75-8915
α-helix90-945
α-helix95-10410
α-helix111-14232
α-helix146-1527
α-helix155-17824
β-strand18314
α-helix187-1948
β-strand20314
α-helix205-2128
α-helix213-2175
α-helix218-23518
α-helix285-31531
α-helix322-34322
α-helix347-35610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BETA1 adrenergic receptorA, B, C, Dprotein313MELEAGRIS GALLOPAVOP07700 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2VT4_1 BETA1 ADRENERGIC RECEPTOR (chains A, B, C, D)
MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVV
GLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQ
SLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIA
SSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFT
LCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLAFP
RKADRRLHHHHHH

Ligands and cofactors

IDNameFormulaCopies
D10DecaneC10 H222
SOGoctyl 1-thio-beta-D-glucopyranosideC14 H28 O5 S12
P32CyanopindololC16 H21 N3 O24

Water and common crystallization additives (NA) are not listed.

Primary citation

Structure of a Beta1-Adrenergic G-Protein-Coupled Receptor. Warne, A., Serrano-Vega, M.J., Baker, J.G. et al. Nature (2008) 454:486. DOI 10.1038/NATURE07101 · PubMed

Other PDB entries of the same protein (UniProt P07700 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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