Structure of C3d Bound to a Fragment of FHR-2 and S. aureus Efb-C. Determined by X-ray diffraction at 3.3 Å resolution. Released 10 Dec 2025.
Explore 9N20 in 3D Show helices and sheets RCSB PDB PDBe
9N20 contains 27 α-helices and 24 β-strands across 3 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 | 999-1003 | 5 | |
| α-helix | 1013-1031 | 19 | |
| α-helix | 1034-1037 | 4 | |
| α-helix | 1040-1056 | 17 | |
| α-helix | 1057-1059 | 3 | |
| β-strand | 1060 | 1 | 1 |
| β-strand | 1066 | 1 | 1 |
| α-helix | 1073-1075 | 3 | |
| α-helix | 1076-1089 | 14 | |
| α-helix | 1097-1109 | 13 | |
| β-strand | 1112 | 1 | 2 |
| β-strand | 1118 | 1 | 2 |
| α-helix | 1131-1134 | 4 | |
| α-helix | 1139-1153 | 15 | |
| α-helix | 1155-1158 | 4 | |
| α-helix | 1165-1178 | 14 | |
| α-helix | 1186-1199 | 14 | |
| α-helix | 1205-1212 | 8 | |
| β-strand | 1215 | 1 | 3 |
| β-strand | 1219 | 1 | 3 |
| α-helix | 1226-1243 | 18 | |
| α-helix | 1249-1258 | 10 | |
| α-helix | 1269-1284 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 149 | 1 | 4 |
| α-helix | 151-155 | 5 | |
| β-strand | 158-160 | 3 | 5 |
| α-helix | 163-165 | 3 | |
| β-strand | 168 | 1 | 4 |
| β-strand | 174-175 | 2 | 6 |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 182 | 1 | |
| β-strand | 183-185 | 3 | 7 |
| β-strand | 189-190 | 2 | 6 |
| α-helix | 197-198 | 2 | |
| β-strand | 202-204 | 3 | 7 |
| β-strand | 207-208 | 2 | 8 |
| α-helix | 211-217 | 7 | |
| β-strand | 219-221 | 3 | 9 |
| β-strand | 230-231 | 2 | 8 |
| β-strand | 237-238 | 2 | 10 |
| β-strand | 239-241 | 3 | 9 |
| β-strand | 246-247 | 2 | 11 |
| β-strand | 254-255 | 2 | 10 |
| β-strand | 258 | 1 | 12 |
| β-strand | 261 | 1 | 12 |
| α-helix | 263-265 | 3 | |
| β-strand | 267-268 | 2 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-123 | 22 | |
| α-helix | 127-138 | 12 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-161 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C3dg fragment | A | protein | 297 | Homo sapiens | P01024 (AlphaFold model) |
| Fibrinogen-binding protein | C | protein | 75 | Staphylococcus aureus subsp. aureus Mu50 | P68799 (AlphaFold model) |
| Complement factor H-related protein 2 | B | protein | 131 | Homo sapiens | P36980 (AlphaFold model) |
>9N20_1 Complement C3dg fragment (chains A) GSRSTDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIK KGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILE KQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSIT KAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNV EATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP
>9N20_2 Fibrinogen-binding protein (chains C) GSTFNKPAAKTDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMV LQERIDNVLKQGLVR
>9N20_3 Complement factor H-related protein 2 (chains B) 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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