Structure of C3d Bound to a Fragment of FHR-2. Determined by X-ray diffraction at 2.31 Å resolution. Released 10 Dec 2025.
Explore 9N1Z in 3D Show helices and sheets RCSB PDB PDBe
9N1Z contains 49 α-helices and 52 β-strands across 4 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 | 994-996 | 3 | |
| α-helix | 998-1003 | 6 | |
| α-helix | 1013-1031 | 19 | |
| α-helix | 1034-1037 | 4 | |
| α-helix | 1039-1057 | 19 | |
| β-strand | 1060 | 1 | 1 |
| β-strand | 1066 | 1 | 1 |
| α-helix | 1073-1075 | 3 | |
| α-helix | 1076-1089 | 14 | |
| α-helix | 1097-1110 | 14 | |
| β-strand | 1112 | 1 | 2 |
| β-strand | 1118 | 1 | 2 |
| α-helix | 1127-1129 | 3 | |
| α-helix | 1131-1134 | 4 | |
| α-helix | 1139-1153 | 15 | |
| α-helix | 1155-1158 | 4 | |
| α-helix | 1165-1179 | 15 | |
| α-helix | 1186-1197 | 12 | |
| α-helix | 1205-1212 | 8 | |
| β-strand | 1215 | 1 | 3 |
| β-strand | 1219 | 1 | 3 |
| α-helix | 1226-1243 | 18 | |
| α-helix | 1249-1259 | 11 | |
| α-helix | 1269-1284 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 147-148 | 2 | |
| β-strand | 149 | 1 | 4 |
| α-helix | 152-154 | 3 | |
| β-strand | 158-160 | 3 | 5 |
| β-strand | 168 | 1 | 4 |
| β-strand | 173-175 | 3 | 6 |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 179 | 1 | |
| α-helix | 182 | 1 | |
| β-strand | 183-185 | 3 | 7 |
| β-strand | 189-191 | 3 | 6 |
| β-strand | 192-193 | 2 | 8 |
| β-strand | 196-197 | 2 | 8 |
| α-helix | 198-201 | 4 | |
| β-strand | 202-204 | 3 | 7 |
| β-strand | 207-209 | 3 | 9 |
| α-helix | 211-217 | 7 | |
| β-strand | 219-221 | 3 | 10 |
| β-strand | 229-231 | 3 | 9 |
| β-strand | 236-238 | 3 | 11 |
| β-strand | 239-241 | 3 | 10 |
| α-helix | 242 | 1 | |
| β-strand | 246-247 | 2 | 12 |
| β-strand | 254-256 | 3 | 11 |
| β-strand | 258 | 1 | 13 |
| β-strand | 261 | 1 | 13 |
| β-strand | 267-268 | 2 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1013-1031 | 19 | |
| α-helix | 1034-1037 | 4 | |
| α-helix | 1043-1057 | 15 | |
| β-strand | 1060 | 1 | 14 |
| β-strand | 1066 | 1 | 14 |
| α-helix | 1073-1075 | 3 | |
| α-helix | 1076-1089 | 14 | |
| α-helix | 1094-1096 | 3 | |
| α-helix | 1097-1110 | 14 | |
| β-strand | 1112 | 1 | 15 |
| β-strand | 1118 | 1 | 15 |
| α-helix | 1127-1129 | 3 | |
| α-helix | 1139-1153 | 15 | |
| α-helix | 1165-1179 | 15 | |
| α-helix | 1180-1182 | 3 | |
| α-helix | 1186-1198 | 13 | |
| α-helix | 1205-1212 | 8 | |
| β-strand | 1215 | 1 | 16 |
| β-strand | 1219 | 1 | 16 |
| α-helix | 1229-1242 | 14 | |
| α-helix | 1249-1257 | 9 | |
| α-helix | 1269-1284 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 149 | 1 | 17 |
| α-helix | 152-154 | 3 | |
| β-strand | 158-160 | 3 | 18 |
| α-helix | 163-165 | 3 | |
| β-strand | 168 | 1 | 17 |
| β-strand | 173-175 | 3 | 19 |
| β-strand | 176-178 | 3 | 18 |
| α-helix | 179 | 1 | |
| α-helix | 182 | 1 | |
| β-strand | 183-185 | 3 | 20 |
| β-strand | 189-191 | 3 | 19 |
| β-strand | 192-193 | 2 | 21 |
| β-strand | 196-197 | 2 | 21 |
| α-helix | 198-201 | 4 | |
| β-strand | 202-204 | 3 | 20 |
| β-strand | 207-208 | 2 | 22 |
| α-helix | 211-216 | 6 | |
| β-strand | 219-221 | 3 | 23 |
| β-strand | 230-231 | 2 | 22 |
| β-strand | 236-238 | 3 | 24 |
| β-strand | 239-241 | 3 | 23 |
| α-helix | 242 | 1 | |
| β-strand | 246-247 | 2 | 25 |
| β-strand | 254-256 | 3 | 24 |
| α-helix | 257 | 1 | |
| β-strand | 258 | 1 | 26 |
| β-strand | 261 | 1 | 26 |
| β-strand | 267-268 | 2 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C3dg fragment | A, C | protein | 297 | Homo sapiens | P01024 (AlphaFold model) |
| Complement factor H-related protein 2 | B, D | protein | 131 | Homo sapiens | P36980 (AlphaFold model) |
>9N1Z_1 Complement C3dg fragment (chains A, C) GSRSTDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIK KGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILE KQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSIT KAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNV EATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP
>9N1Z_2 Complement factor H-related protein 2 (chains B, D) GSTGSSAEKCGPPPPIDNGDITSFLLSVYAPGSSVEYQCQNLYQLEGNNQITCRNGQWSE PPKCLDPCVISQEIMEKYNIKLKWTNQQKLYSRTGDIVEFVCKSGYHPTKSHSFRAMCQN GKLVYPSCEEK
The C-terminal domain of Staphylococcus aureus Efb recruits FHR-2 to C3b, synergistically inhibiting the terminal complement pathway. Duan, H., Kortvely, E., Mary, J.L. et al. J Immunol (2026) 215. DOI 10.1093/jimmun/vkaf316 · PubMed
Other PDB entries of the same protein (UniProt P01024 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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