Crystal structure of N-glycosylated human calcitonin receptor extracellular domain in complex with salmon calcitonin (22-32). Determined by X-ray diffraction at 2.85 Å resolution. Released 12 Feb 2020.
Explore 6PGQ in 3D Show helices and sheets RCSB PDB PDBe
6PGQ contains 31 α-helices and 35 β-strands across 2 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 | -331--330 | 2 | |
| β-strand | -326--323 | 4 | 1 |
| α-helix | -316--302 | 15 | |
| β-strand | -298--295 | 4 | 1 |
| α-helix | -290--283 | 8 | |
| β-strand | -274--270 | 5 | 1 |
| α-helix | -269--267 | 3 | |
| α-helix | -266--261 | 6 | |
| β-strand | -257 | 1 | 2 |
| α-helix | -256--254 | 3 | |
| α-helix | -250--246 | 5 | |
| β-strand | -244 | 1 | 3 |
| α-helix | -242--237 | 6 | |
| β-strand | -235--234 | 2 | 4 |
| β-strand | -231--230 | 2 | 4 |
| β-strand | -227--222 | 6 | 1 |
| β-strand | -219--215 | 5 | 5 |
| β-strand | -205 | 1 | 6 |
| α-helix | -204--202 | 3 | |
| α-helix | -201--192 | 10 | |
| β-strand | -188--186 | 3 | 5 |
| α-helix | -179--170 | 10 | |
| β-strand | -166--161 | 6 | 7 |
| β-strand | -158--151 | 8 | 7 |
| α-helix | -147--133 | 15 | |
| α-helix | -123--115 | 9 | |
| β-strand | -111--106 | 6 | 5 |
| α-helix | -104--102 | 3 | |
| α-helix | -101--95 | 7 | |
| β-strand | -91--88 | 4 | 5 |
| α-helix | -87--85 | 3 | |
| β-strand | -84 | 1 | 6 |
| β-strand | -83 | 1 | 8 |
| β-strand | -80 | 1 | 8 |
| α-helix | -76 | 1 | |
| β-strand | -75--74 | 2 | 9 |
| β-strand | -73--67 | 7 | 1 |
| β-strand | -66 | 1 | 2 |
| α-helix | -60--54 | 7 | |
| α-helix | -53--49 | 5 | |
| α-helix | -46--37 | 10 | |
| β-strand | -32--31 | 2 | 1 |
| β-strand | -29 | 1 | 3 |
| α-helix | -28--22 | 7 | |
| α-helix | -18--7 | 12 | |
| β-strand | -5--4 | 2 | 9 |
| α-helix | -3--2 | 2 | |
| α-helix | 3-18 | 16 | |
| α-helix | 24-35 | 12 | |
| α-helix | 37-61 | 25 | |
| α-helix | 63-64 | 2 | |
| β-strand | 71-72 | 2 | 10 |
| α-helix | 73-74 | 2 | |
| β-strand | 75-76 | 2 | 11 |
| β-strand | 81-82 | 2 | 11 |
| β-strand | 85-86 | 2 | 10 |
| β-strand | 90-94 | 5 | 12 |
| α-helix | 95-96 | 2 | |
| β-strand | 107-111 | 5 | 12 |
| β-strand | 112 | 1 | 13 |
| α-helix | 113 | 1 | |
| β-strand | 118 | 1 | 13 |
| β-strand | 120 | 1 | 14 |
| β-strand | 127 | 1 | 14 |
| β-strand | 130 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-26 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltodextrin-binding protein,Calcitonin receptor | A | protein | 482 | Escherichia coli, Homo sapiens | P30988 (AlphaFold model) |
| Calcitonin | B | protein | 12 | Oncorhynchus sp. | P01263 (AlphaFold model) |
>6PGQ_1 Maltodextrin-binding protein,Calcitonin receptor (chains A) MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD EALKDAQTNAAAEFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDT PAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKHHHH HH
>6PGQ_2 Calcitonin (chains B) YPRTNTGSGTPX
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (ACT) are not listed.
Calcitonin Receptor N-Glycosylation Enhances Peptide Hormone Affinity by Controlling Receptor Dynamics. Lee, S.M., Jeong, Y., Simms, J. et al. J Mol Biol (2020) 432:1996-2014. DOI 10.1016/j.jmb.2020.01.028 · PubMed
Other PDB entries of the same protein (UniProt P30988 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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