Turkey BETA1 adrenergic receptor with stabilising mutations and bound cyanopindolol. Determined by X-ray diffraction at 2.7 Å resolution. Released 24 Jun 2008.
Explore 2VT4 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-68 | 28 | |
| α-helix | 70-72 | 3 | |
| α-helix | 75-89 | 15 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-104 | 10 | |
| α-helix | 111-142 | 32 | |
| α-helix | 146-152 | 7 | |
| α-helix | 155-178 | 24 | |
| β-strand | 183 | 1 | 1 |
| α-helix | 187-194 | 8 | |
| β-strand | 203 | 1 | 1 |
| α-helix | 205-212 | 8 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-235 | 18 | |
| α-helix | 285-315 | 31 | |
| α-helix | 322-343 | 22 | |
| α-helix | 347-356 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-68 | 29 | |
| α-helix | 75-89 | 15 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-104 | 10 | |
| α-helix | 111-144 | 34 | |
| α-helix | 146-152 | 7 | |
| α-helix | 155-169 | 15 | |
| α-helix | 170-174 | 5 | |
| α-helix | 175-178 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 187-194 | 8 | |
| β-strand | 203 | 1 | 2 |
| α-helix | 205-212 | 8 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-235 | 18 | |
| α-helix | 285-315 | 31 | |
| α-helix | 322-342 | 21 | |
| α-helix | 343-345 | 3 | |
| α-helix | 347-356 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-68 | 29 | |
| α-helix | 75-89 | 15 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-104 | 10 | |
| α-helix | 111-144 | 34 | |
| α-helix | 146-152 | 7 | |
| α-helix | 155-169 | 15 | |
| α-helix | 170-174 | 5 | |
| α-helix | 175-178 | 4 | |
| β-strand | 183 | 1 | 3 |
| α-helix | 187-194 | 8 | |
| β-strand | 203 | 1 | 3 |
| α-helix | 205-212 | 8 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-235 | 18 | |
| α-helix | 285-315 | 31 | |
| α-helix | 322-342 | 21 | |
| α-helix | 343-345 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-68 | 27 | |
| α-helix | 70-72 | 3 | |
| α-helix | 75-89 | 15 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-104 | 10 | |
| α-helix | 111-142 | 32 | |
| α-helix | 146-152 | 7 | |
| α-helix | 155-178 | 24 | |
| β-strand | 183 | 1 | 4 |
| α-helix | 187-194 | 8 | |
| β-strand | 203 | 1 | 4 |
| α-helix | 205-212 | 8 | |
| α-helix | 213-217 | 5 | |
| α-helix | 218-235 | 18 | |
| α-helix | 285-315 | 31 | |
| α-helix | 322-343 | 22 | |
| α-helix | 347-356 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BETA1 adrenergic receptor | A, B, C, D | protein | 313 | MELEAGRIS GALLOPAVO | P07700 (AlphaFold model) |
>2VT4_1 BETA1 ADRENERGIC RECEPTOR (chains A, B, C, D) MGAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRLQTLTNLFITSLACADLVV GLLVVPFGATLVVRGTWLWGSFLCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQ SLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIA SSIISFYIPLLIMIFVALRVYREAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFT LCWLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPIIYCRSPDFRKAFKRLLAFP RKADRRLHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| D10 | Decane | C10 H22 | 2 |
| SOG | octyl 1-thio-beta-D-glucopyranoside | C14 H28 O5 S | 12 |
| P32 | Cyanopindolol | C16 H21 N3 O2 | 4 |
Water and common crystallization additives (NA) are not listed.
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:
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