Crystal structure of a class A GPCR. Determined by X-ray diffraction at 3.2 Å resolution. Released 2 Sept 2020.
Explore 6LFL in 3D Show helices and sheets RCSB PDB PDBe
6LFL contains 22 α-helices and 10 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 | 48-75 | 28 | |
| α-helix | 82-109 | 28 | |
| α-helix | 116-148 | 33 | |
| α-helix | 161-176 | 16 | |
| α-helix | 180-183 | 4 | |
| β-strand | 185-187 | 3 | 1 |
| α-helix | 193-194 | 2 | |
| β-strand | 195-197 | 3 | 1 |
| α-helix | 206-216 | 11 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-240 | 19 | |
| α-helix | 1016-1026 | 11 | |
| β-strand | 1033-1037 | 5 | 2 |
| β-strand | 1041 | 1 | 3 |
| α-helix | 1048-1058 | 11 | |
| α-helix | 1062-1066 | 5 | |
| β-strand | 1067-1072 | 6 | 2 |
| β-strand | 1075 | 1 | 3 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 2 |
| α-helix | 1102-1111 | 10 | |
| β-strand | 1114-1117 | 4 | 2 |
| α-helix | 1126-1133 | 8 | |
| β-strand | 1137-1141 | 5 | 2 |
| α-helix | 1146-1149 | 4 | |
| β-strand | 1156-1158 | 3 | 2 |
| α-helix | 1163-1176 | 14 | |
| α-helix | 1182-1196 | 15 | |
| α-helix | 247-278 | 32 | |
| α-helix | 290-306 | 17 | |
| α-helix | 309-316 | 8 | |
| α-helix | 319-331 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C-X-C chemokine receptor type 2,GlgA glycogen synthase,C-X-C chemokine receptor type 2 | A | protein | 502 | Homo sapiens, Pyrococcus abyssi (strain GE5 / Orsay) | P25025 (AlphaFold model), Q9V2J8 (AlphaFold model) |
>6LFL_1 C-X-C chemokine receptor type 2,GlgA glycogen synthase,C-X-C chemokine receptor type 2 (chains A) APCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLL FALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGIWLLACISVDRYLAIVHATRTLT QKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQ SFGFIVPLLIMLFCYGFTLRTLFKAGIDCSFWNESYLTGSRDERKKSLLSKFGMDEGVTF MFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELEGWARSLEEKHGNVKV ITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETG ILVKAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSGQKHREMRVIFAVVLIFLL CWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILAILHSCLNPLIYAFIGQKFR HGLLKILAIHGLISKDSLPKDS
| ID | Name | Formula | Copies |
|---|---|---|---|
| EBX | 4-[[3,4-bis(oxidanylidene)-2-[[(1~{R})-1-(4-propan-2-ylfuran-2-yl)propyl]amino]… | C22 H26 N4 O5 | 1 |
Structural basis of CXC chemokine receptor 2 activation and signalling. Liu, K., Wu, L., Yuan, S. et al. Nature (2020) 585:135-140. DOI 10.1038/s41586-020-2492-5 · PubMed
Other PDB entries of the same protein (UniProt P25025 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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