The Crystal Structure of C2b, a Fragment of Complement Component C2 produced during C3-convertase Formation. Determined by X-ray diffraction at 1.8 Å resolution. Released 10 Mar 2009.
Explore 3ERB in 3D Show helices and sheets RCSB PDB PDBe
3ERB contains 5 α-helices and 23 β-strands across 1 chain. 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 | 11 | 1 | 1 |
| β-strand | 14-17 | 4 | 2 |
| α-helix | 25 | 1 | |
| β-strand | 26-30 | 5 | 2 |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 41-44 | 4 | 2 |
| β-strand | 50-51 | 2 | 2 |
| β-strand | 63-66 | 4 | 1 |
| β-strand | 68-70 | 3 | 3 |
| α-helix | 71-72 | 2 | |
| β-strand | 78-81 | 4 | 4 |
| β-strand | 86-88 | 3 | 3 |
| β-strand | 92-97 | 6 | 4 |
| α-helix | 98 | 1 | |
| β-strand | 102-104 | 3 | 5 |
| β-strand | 108-110 | 3 | 4 |
| β-strand | 111 | 1 | 6 |
| β-strand | 117 | 1 | 6 |
| β-strand | 123-125 | 3 | 5 |
| α-helix | 132-133 | 2 | |
| β-strand | 140-143 | 4 | 7 |
| β-strand | 152-157 | 6 | 7 |
| β-strand | 162-164 | 3 | 8 |
| β-strand | 168-170 | 3 | 7 |
| β-strand | 171 | 1 | 9 |
| β-strand | 177 | 1 | 9 |
| β-strand | 183-185 | 3 | 8 |
| α-helix | 187-191 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement C2 | A | protein | 223 | Homo sapiens | P06681 (AlphaFold model) |
>3ERB_1 Complement C2 (chains A) APSCPQNVNISGGTFTLSHGWAPGSLLTYSCPQGLYPSPASRLCKSSGQWQTPGATRSLS KAVCKPVRCPAPVSFENGIYTPRLGSYPVGGNVSFECEDGFILRGSPVRQCRPNGMWDGE TAVCDNGAGHCPNPGISLGAVRTGFRFGHGDKVRYRCSSNLVLTGSSERECQGNGVWSGT EPICRQPYSYDFPEDVAPALGTSFSHMLGATNPTQKTKESLGR
The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation. Krishnan, V., Xu, Y., Macon, K. et al. Acta Crystallogr D Biol Crystallogr (2009) 65:266-274. DOI 10.1107/S0907444909000389 · PubMed
Other PDB entries of the same protein (UniProt P06681 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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