Crystal structure of human rage ligand-binding domain. Determined by X-ray diffraction at 1.85 Å resolution. Released 24 Mar 2009.
Explore 3CJJ in 3D Show helices and sheets RCSB PDB PDBe
3CJJ contains 7 α-helices and 21 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 |
|---|---|---|---|
| α-helix | 23 | 1 | |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 34-36 | 3 | 2 |
| β-strand | 49-55 | 7 | 1 |
| β-strand | 62-64 | 3 | 1 |
| β-strand | 77-78 | 2 | 2 |
| β-strand | 84-86 | 3 | 2 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-102 | 8 | 1 |
| β-strand | 108-118 | 11 | 1 |
| β-strand | 119 | 1 | 3 |
| α-helix | 122-124 | 3 | |
| β-strand | 125-127 | 3 | 4 |
| β-strand | 132-134 | 3 | 5 |
| β-strand | 139-149 | 11 | 4 |
| β-strand | 150 | 1 | 3 |
| β-strand | 154-159 | 6 | 6 |
| β-strand | 162-163 | 2 | 6 |
| α-helix | 164-165 | 2 | |
| β-strand | 171-179 | 9 | 4 |
| β-strand | 186-194 | 9 | 4 |
| α-helix | 196-197 | 2 | |
| β-strand | 206-211 | 6 | 6 |
| β-strand | 220-221 | 2 | 6 |
| α-helix | 222-224 | 3 | |
| β-strand | 225 | 1 | 6 |
| α-helix | 227 | 1 | |
| β-strand | 228-230 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Advanced glycosylation end product-specific receptor | A | protein | 219 | Homo sapiens | Q15109 (AlphaFold model) |
>3CJJ_1 Advanced glycosylation end product-specific receptor (chains A) MAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPN GSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKV GTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGD PRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (ACT) are not listed.
Structural basis for ligand recognition and activation of RAGE. Koch, M., Chitayat, S., Dattilo, B.M. et al. Structure (2010) 18:1342-1352. DOI 10.1016/j.str.2010.05.017 · PubMed
Other PDB entries of the same protein (UniProt Q15109 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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