Crystal structure of Efb-C / C3d Complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 Mar 2007.
Explore 2GOX in 3D Show helices and sheets RCSB PDB PDBe
2GOX contains 46 α-helices and 12 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 | 993-996 | 4 | |
| α-helix | 997-1003 | 7 | |
| α-helix | 1013-1030 | 18 | |
| 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 | 1097-1111 | 15 | |
| β-strand | 1112 | 1 | 2 |
| β-strand | 1118 | 1 | 2 |
| α-helix | 1127-1129 | 3 | |
| α-helix | 1131-1134 | 4 | |
| α-helix | 1139-1158 | 20 | |
| α-helix | 1165-1179 | 15 | |
| α-helix | 1180-1182 | 3 | |
| α-helix | 1186-1198 | 13 | |
| α-helix | 1204-1213 | 10 | |
| β-strand | 1215 | 1 | 3 |
| β-strand | 1219 | 1 | 3 |
| α-helix | 1226-1243 | 18 | |
| α-helix | 1249-1257 | 9 | |
| α-helix | 1269-1285 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-124 | 23 | |
| α-helix | 127-139 | 13 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-161 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 994-996 | 3 | |
| α-helix | 997-1003 | 7 | |
| α-helix | 1013-1030 | 18 | |
| α-helix | 1034-1037 | 4 | |
| α-helix | 1039-1056 | 18 | |
| α-helix | 1057-1059 | 3 | |
| β-strand | 1060 | 1 | 4 |
| β-strand | 1066 | 1 | 4 |
| α-helix | 1073-1075 | 3 | |
| α-helix | 1076-1088 | 13 | |
| α-helix | 1089-1091 | 3 | |
| α-helix | 1097-1106 | 10 | |
| α-helix | 1107-1111 | 5 | |
| β-strand | 1112 | 1 | 5 |
| β-strand | 1118 | 1 | 5 |
| α-helix | 1127-1129 | 3 | |
| α-helix | 1131-1134 | 4 | |
| α-helix | 1139-1158 | 20 | |
| α-helix | 1165-1179 | 15 | |
| α-helix | 1180-1182 | 3 | |
| α-helix | 1186-1198 | 13 | |
| α-helix | 1204-1213 | 10 | |
| β-strand | 1215 | 1 | 6 |
| β-strand | 1219 | 1 | 6 |
| α-helix | 1226-1242 | 17 | |
| α-helix | 1249-1259 | 11 | |
| α-helix | 1269-1285 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 103-124 | 22 | |
| α-helix | 127-139 | 13 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-161 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C3 | A, C | protein | 297 | Homo sapiens | P01024 (AlphaFold model) |
| Fibrinogen-binding protein | B, D | protein | 65 | Staphylococcus aureus subsp. aureus Mu50 | P68799 (AlphaFold model) |
>2GOX_1 Complement C3 (chains A, C) GSRSTDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIK KGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILE KQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSIT KAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNV EATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP
>2GOX_2 Fibrinogen-binding protein (chains B, D) TDATIKKEQKLIQAQNLVREFEKTHTVSAHRKAQKAVNLVSFEYKVKKMVLQERIDNVLK QGLVR
A structural basis for complement inhibition by Staphylococcus aureus. Hammel, M., Sfyroera, G., Ricklin, D. et al. Nat Immunol (2007) 8:430-437. DOI 10.1038/ni1450 · 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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