CR2-C3D complex structure. Determined by X-ray diffraction at 2.04 Å resolution. Released 13 Jun 2001.
Explore 1GHQ in 3D Show helices and sheets RCSB PDB PDBe
1GHQ contains 29 α-helices and 46 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 |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| α-helix | 4-8 | 5 | |
| α-helix | 20-38 | 19 | |
| α-helix | 41-44 | 4 | |
| α-helix | 46-48 | 3 | |
| α-helix | 49-64 | 16 | |
| β-strand | 67 | 1 | 2 |
| β-strand | 73 | 1 | 2 |
| α-helix | 80-82 | 3 | |
| α-helix | 83-96 | 14 | |
| α-helix | 104-118 | 15 | |
| β-strand | 119 | 1 | 3 |
| β-strand | 125 | 1 | 3 |
| α-helix | 134-141 | 8 | |
| α-helix | 146-165 | 20 | |
| α-helix | 172-186 | 15 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-205 | 13 | |
| α-helix | 211-220 | 10 | |
| β-strand | 222 | 1 | 4 |
| β-strand | 226 | 1 | 4 |
| α-helix | 236-250 | 15 | |
| α-helix | 256-265 | 10 | |
| α-helix | 276-292 | 17 | |
| α-helix | 293-295 | 3 | |
| α-helix | 305 | 1 | |
| β-strand | 306 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 5 |
| α-helix | 7-9 | 3 | |
| β-strand | 13-15 | 3 | 6 |
| β-strand | 22-23 | 2 | 5 |
| β-strand | 27-29 | 3 | 7 |
| β-strand | 30-32 | 3 | 6 |
| β-strand | 36-39 | 4 | 8 |
| β-strand | 43-45 | 3 | 7 |
| β-strand | 46-47 | 2 | 9 |
| β-strand | 55-56 | 2 | 9 |
| β-strand | 62-65 | 4 | 8 |
| β-strand | 71 | 1 | 10 |
| α-helix | 73-75 | 3 | |
| β-strand | 80-84 | 5 | 11 |
| β-strand | 90 | 1 | 10 |
| β-strand | 94-99 | 6 | 11 |
| α-helix | 100 | 1 | |
| β-strand | 104-106 | 3 | 12 |
| β-strand | 110-112 | 3 | 11 |
| β-strand | 113 | 1 | 13 |
| β-strand | 119 | 1 | 13 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-128 | 3 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 14 |
| α-helix | 7-9 | 3 | |
| β-strand | 13-15 | 3 | 15 |
| β-strand | 22-23 | 2 | 14 |
| β-strand | 27-29 | 3 | 16 |
| β-strand | 30-32 | 3 | 15 |
| β-strand | 36-39 | 4 | 17 |
| β-strand | 43-45 | 3 | 16 |
| β-strand | 46-47 | 2 | 18 |
| β-strand | 55-56 | 2 | 18 |
| α-helix | 59-61 | 3 | |
| β-strand | 62-65 | 4 | 17 |
| α-helix | 66 | 1 | |
| β-strand | 71-72 | 2 | 19 |
| α-helix | 73-75 | 3 | |
| β-strand | 80-84 | 5 | 20 |
| β-strand | 89-90 | 2 | 19 |
| β-strand | 94-99 | 6 | 20 |
| α-helix | 100 | 1 | |
| β-strand | 103-106 | 4 | 21 |
| β-strand | 110-112 | 3 | 20 |
| β-strand | 113 | 1 | 22 |
| β-strand | 119 | 1 | 22 |
| α-helix | 123-125 | 3 | |
| β-strand | 126-129 | 4 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C3 | A | protein | 308 | Homo sapiens | P01024 (AlphaFold model) |
| CR2/CD121/C3D/EPSTEIN-barr virus receptor | B, C | protein | 134 | Homo sapiens | P20023 (AlphaFold model) |
>1GHQ_1 COMPLEMENT C3 (chains A) MLDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGY TQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQK PDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAG DFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEAT SYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPSDHQEL NLDVSLQL
>1GHQ_2 CR2/CD121/C3D/EPSTEIN-BARR VIRUS RECEPTOR (chains B, C) AISCGSPPPILNGRISYYSTPIAVGTVIRYSCSGTFRLIGEKSLLCITKDKVDGTWDKPA PKCEYFNKYSSCPEPIVPGGYKIRGSTPYRHGDSVTFACKTNFSMNGNKSVWCQANNMWG PTRLPTCVSVFPLE
Structure of complement receptor 2 in complex with its C3d ligand. Szakonyi, G., Guthridge, J.M., Li, D. et al. Science (2001) 292:1725-1728. DOI 10.1126/science.1059118 · 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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