NPFF bound Mas1 Receptor Complex. Determined by electron microscopy at 2.54 Å resolution. Released 15 Apr 2026.
Explore 9X3Z in 3D Show helices and sheets RCSB PDB PDBe
9X3Z contains 37 α-helices and 58 β-strands across 5 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 | 7-32 | 26 | |
| β-strand | 33-40 | 8 | 1 |
| α-helix | 46-52 | 7 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 211-215 | 5 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 233-244 | 12 | |
| α-helix | 247-249 | 3 | |
| β-strand | 254-259 | 6 | 1 |
| α-helix | 261-267 | 7 | |
| α-helix | 299-317 | 19 | |
| β-strand | 326-330 | 5 | 1 |
| α-helix | 338-357 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-30 | 19 | |
| α-helix | 35-38 | 4 | |
| α-helix | 43-44 | 2 | |
| β-strand | 52-56 | 5 | 2 |
| β-strand | 63-68 | 6 | 3 |
| β-strand | 74-79 | 6 | 3 |
| β-strand | 83-88 | 6 | 3 |
| β-strand | 94-99 | 6 | 3 |
| β-strand | 105-110 | 6 | 4 |
| β-strand | 116-121 | 6 | 4 |
| β-strand | 126-130 | 5 | 4 |
| β-strand | 139-144 | 6 | 4 |
| β-strand | 151-156 | 6 | 5 |
| β-strand | 161-166 | 6 | 5 |
| β-strand | 171-175 | 5 | 5 |
| β-strand | 180-185 | 6 | 5 |
| β-strand | 192-197 | 6 | 6 |
| β-strand | 203-208 | 6 | 6 |
| β-strand | 213-217 | 5 | 6 |
| β-strand | 223-227 | 5 | 6 |
| β-strand | 234-239 | 6 | 7 |
| β-strand | 245-250 | 6 | 7 |
| β-strand | 255-259 | 5 | 7 |
| β-strand | 264-269 | 6 | 7 |
| α-helix | 277 | 1 | |
| β-strand | 278-283 | 6 | 8 |
| β-strand | 289-294 | 6 | 8 |
| β-strand | 299-303 | 5 | 8 |
| β-strand | 309-313 | 5 | 8 |
| β-strand | 320-325 | 6 | 2 |
| β-strand | 332-336 | 5 | 2 |
| β-strand | 341-344 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-23 | 15 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
| α-helix | 56-58 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-59 | 26 | |
| α-helix | 65-92 | 28 | |
| α-helix | 102-135 | 34 | |
| α-helix | 137-142 | 6 | |
| α-helix | 148-166 | 19 | |
| α-helix | 167-172 | 6 | |
| α-helix | 182-193 | 12 | |
| α-helix | 194-199 | 6 | |
| α-helix | 200-215 | 16 | |
| α-helix | 226-236 | 11 | |
| α-helix | 237-241 | 5 | |
| α-helix | 242-254 | 13 | |
| α-helix | 261-277 | 17 | |
| α-helix | 278-282 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 9 |
| β-strand | 10-12 | 3 | 10 |
| β-strand | 17-25 | 9 | 9 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 10 |
| β-strand | 45-51 | 7 | 10 |
| β-strand | 58-60 | 3 | 10 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 78-84 | 7 | 9 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 10 |
| β-strand | 110-111 | 2 | 10 |
| β-strand | 115-119 | 5 | 10 |
| α-helix | 138-139 | 2 | |
| β-strand | 140-141 | 2 | 11 |
| β-strand | 146 | 1 | 12 |
| β-strand | 155-161 | 7 | 11 |
| β-strand | 166 | 1 | 13 |
| β-strand | 172 | 1 | 13 |
| β-strand | 174-179 | 6 | 12 |
| β-strand | 186-190 | 5 | 12 |
| β-strand | 194-195 | 2 | 12 |
| α-helix | 196 | 1 | |
| β-strand | 203-207 | 5 | 11 |
| β-strand | 211-216 | 6 | 11 |
| α-helix | 221-223 | 3 | |
| β-strand | 226-231 | 6 | 12 |
| β-strand | 238-239 | 2 | 12 |
| β-strand | 243-244 | 2 | 12 |
Structural insight into ligand binding and activation of the orphan GPCR Mas1. Zhang, Y., Wang, Q., Liu, H. et al. EMBO J (2026) 45:3500-3513. DOI 10.1038/s44318-026-00764-6 · PubMed
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