Crystal structure of human pituitary adenylate cyclase 1 Receptor-short N-terminal extracellular domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Jun 2011.
Explore 3N94 in 3D Show helices and sheets RCSB PDB PDBe
3N94 contains 30 α-helices and 33 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -342--338 | 5 | 1 |
| α-helix | -331--317 | 15 | |
| β-strand | -314--310 | 5 | 1 |
| α-helix | -305--296 | 10 | |
| β-strand | -289--285 | 5 | 1 |
| α-helix | -284--282 | 3 | |
| α-helix | -281--276 | 6 | |
| β-strand | -272 | 1 | 2 |
| α-helix | -271--269 | 3 | |
| α-helix | -265--262 | 4 | |
| β-strand | -259 | 1 | 3 |
| α-helix | -257--252 | 6 | |
| β-strand | -250--249 | 2 | 4 |
| β-strand | -246--245 | 2 | 4 |
| β-strand | -242--237 | 6 | 1 |
| β-strand | -234--230 | 5 | 5 |
| β-strand | -220 | 1 | 6 |
| α-helix | -219--217 | 3 | |
| α-helix | -216--208 | 9 | |
| β-strand | -203--201 | 3 | 5 |
| α-helix | -194--185 | 10 | |
| β-strand | -181--176 | 6 | 7 |
| β-strand | -173--166 | 8 | 7 |
| α-helix | -162--148 | 15 | |
| α-helix | -138--130 | 9 | |
| β-strand | -126--121 | 6 | 5 |
| α-helix | -119--117 | 3 | |
| α-helix | -116--110 | 7 | |
| β-strand | -106--103 | 4 | 5 |
| α-helix | -102--100 | 3 | |
| β-strand | -99 | 1 | 6 |
| β-strand | -98 | 1 | 8 |
| β-strand | -95 | 1 | 8 |
| α-helix | -94--93 | 2 | |
| β-strand | -90--89 | 2 | 9 |
| β-strand | -88--82 | 7 | 1 |
| β-strand | -81 | 1 | 2 |
| α-helix | -75--70 | 6 | |
| α-helix | -69--64 | 6 | |
| α-helix | -61--52 | 10 | |
| β-strand | -47--46 | 2 | 1 |
| β-strand | -44 | 1 | 3 |
| α-helix | -43--37 | 7 | |
| α-helix | -33--22 | 12 | |
| β-strand | -20--19 | 2 | 9 |
| α-helix | -18--17 | 2 | |
| α-helix | -12-4 | 17 | |
| α-helix | 9-22 | 14 | |
| α-helix | 24-47 | 24 | |
| β-strand | 54 | 1 | 10 |
| β-strand | 57-58 | 2 | 11 |
| β-strand | 63-64 | 2 | 11 |
| β-strand | 67 | 1 | 10 |
| β-strand | 72-76 | 5 | 12 |
| α-helix | 77-78 | 2 | |
| α-helix | 79-83 | 5 | |
| α-helix | 88-90 | 3 | |
| β-strand | 92-96 | 5 | 12 |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 101-102 | 2 | 13 |
| α-helix | 103-105 | 3 | |
| β-strand | 106 | 1 | 12 |
| α-helix | 109-113 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fusion protein of Maltose-binding periplasmic protein and pituitary adenylate cyclase 1… | A | protein | 475 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), P41586 (AlphaFold model) |
>3N94_1 Fusion protein of Maltose-binding periplasmic protein and pituitary adenylate cyclase 1 Receptor-short (chains A) MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAEFAIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVG EMVLVSCPELFRIFNPDQDMGVVSRNCTEDGWSEPFPHYFDACGFDEYEHHHHHH
Crystal Structure of the PAC1R Extracellular Domain Unifies a Consensus Fold for Hormone Recognition by Class B G-Protein Coupled Receptors. Kumar, S., Pioszak, A., Zhang, C. et al. PLoS One (2011) 6:e19682-e19682. DOI 10.1371/journal.pone.0019682 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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