Complex of C-terminal domain of murine complement C3b with the hC3Nb3 nanobody. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Aug 2020.
Explore 6XZU in 3D Show helices and sheets RCSB PDB PDBe
6XZU contains 11 α-helices and 17 β-strands across 2 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 | 4-8 | 5 | 1 |
| β-strand | 11-14 | 4 | 2 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 35-40 | 6 | 2 |
| α-helix | 45-46 | 2 | |
| β-strand | 47-52 | 6 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 2 |
| β-strand | 113-118 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1520-1523 | 4 | |
| α-helix | 1529-1535 | 7 | |
| β-strand | 1541-1554 | 14 | 3 |
| β-strand | 1559-1570 | 12 | 3 |
| β-strand | 1581-1586 | 6 | 3 |
| α-helix | 1588-1590 | 3 | |
| α-helix | 1591-1594 | 4 | |
| β-strand | 1601-1607 | 7 | 3 |
| α-helix | 1608-1610 | 3 | |
| β-strand | 1611-1612 | 2 | 3 |
| β-strand | 1619-1621 | 3 | 3 |
| β-strand | 1627-1631 | 5 | 3 |
| α-helix | 1634-1637 | 4 | |
| α-helix | 1643-1659 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| nanobody hC3Nb1 | A | protein | 127 | Lama glama | |
| Complement C3 | B | protein | 148 | Mus musculus | P01027 (AlphaFold model) |
>6XZU_1 nanobody hC3Nb1 (chains A) MQVQLVESGGGLVQAGGSLRLSCVVSGSTFSDYAMGWYRQAAGEQRELVAAIYSTGRTNY IDSVKGRFTISRDNAKTTVYLQMNSLKPEDTAVYYCNLLGATTMINTKWGQGTQVTVSSL EHHHHHH
>6XZU_2 Complement C3 (chains B) ANCFMQQSQEKINLNVRLDKACEPGVDYVYKTELTNIELLDDFDEYTMTIQQVIKSGSDE VQAGQQRKFISHIKCRNALKLQKGKKYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAE ECQDQKYQKQCEELGAFTESMVVYGCPN
A Complement C3-Specific Nanobody for Modulation of the Alternative Cascade Identifies the C-Terminal Domain of C3b as Functional in C5 Convertase Activity. Pedersen, H., Jensen, R.K., Jensen, J.M.B. et al. J Immunol (2020) 205:2287-2300. DOI 10.4049/jimmunol.2000752 · PubMed
Other PDB entries of the same protein (UniProt P01027 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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