Fusion protein of mbp3-16 and B4 domain of protein A from staphylococcal aureus. Determined by X-ray diffraction at 2.8 Å resolution. Released 30 Mar 2016.
Explore 5CBO in 3D Show helices and sheets RCSB PDB PDBe
5CBO contains 132 α-helices and 0 β-strands across 12 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 | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-88 | 6 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-1228 | 21 | |
| α-helix | 1235-1247 | 13 | |
| α-helix | 1249-1251 | 3 | |
| α-helix | 1252-1263 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-88 | 6 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-1228 | 21 | |
| α-helix | 1235-1247 | 13 | |
| α-helix | 1249-1251 | 3 | |
| α-helix | 1252-1265 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-88 | 6 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-123 | 8 | |
| α-helix | 126-1228 | 21 | |
| α-helix | 1235-1247 | 13 | |
| α-helix | 1249-1251 | 3 | |
| α-helix | 1252-1265 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| mbp3-16,Immunoglobulin G-binding protein A | A, B, C, D, E, F, G, H, I, J, K, L | protein | 176 | synthetic construct, Staphylococcus aureus | P38507 (AlphaFold model) |
>5CBO_1 mbp3-16,Immunoglobulin G-binding protein A (chains A, B, C, D, E, F, G, H, I, J, K, L) SDLGKKLLEAAHAGQDDEVRILMANGADVNAMDNFGVTPLHLAAYWGHFEIVEVLLKYGA DVNASDATGDTPLHLAAKWGYLGIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEI LCKNKAQQAAFYCILHMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQAPK
Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Jeong, W.H., Lee, H., Song, D.H. et al. Nat Commun (2016) 7:11031-11031. DOI 10.1038/ncomms11031 · PubMed
Other PDB entries of the same protein (UniProt P38507 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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