Fusion protein of mbp3-16 and B4 domain of protein A from staphylococcal aureus with chemical cross-linker EY-CBS. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Mar 2016.
Explore 5CBN in 3D Show helices and sheets RCSB PDB PDBe
5CBN contains 35 α-helices and 26 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 |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-57 | 8 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-89 | 7 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-1229 | 22 | |
| α-helix | 1235-1246 | 12 | |
| α-helix | 1252-1265 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| α-helix | 17-31 | 15 | |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 43-51 | 9 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 67-72 | 6 | |
| β-strand | 76 | 1 | 2 |
| α-helix | 77-79 | 3 | |
| α-helix | 83-86 | 4 | |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-95 | 5 | |
| β-strand | 98-99 | 2 | 4 |
| β-strand | 102-103 | 2 | 4 |
| β-strand | 106-111 | 6 | 1 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 128 | 1 | 6 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-141 | 10 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-161 | 8 | |
| β-strand | 167 | 1 | 7 |
| β-strand | 170 | 1 | 8 |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 8 |
| β-strand | 182 | 1 | 7 |
| α-helix | 186-200 | 15 | |
| α-helix | 210-218 | 9 | |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-238 | 7 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 246-248 | 3 | |
| β-strand | 249 | 1 | 6 |
| β-strand | 250 | 1 | 9 |
| β-strand | 253 | 1 | 9 |
| α-helix | 254-255 | 2 | |
| β-strand | 258-259 | 2 | 10 |
| β-strand | 260-266 | 7 | 1 |
| β-strand | 267 | 1 | 2 |
| α-helix | 273-279 | 7 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-296 | 10 | |
| β-strand | 301-302 | 2 | 1 |
| β-strand | 304 | 1 | 3 |
| α-helix | 305-311 | 7 | |
| α-helix | 315-326 | 12 | |
| β-strand | 328-329 | 2 | 10 |
| α-helix | 330-331 | 2 | |
| α-helix | 336-352 | 17 | |
| α-helix | 357-363 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein | B | protein | 369 | Escherichia coli (strain K12) | P0AEX9 (AlphaFold model) |
| mbp3-16,Immunoglobulin G-binding protein A | A | protein | 176 | synthetic construct, Staphylococcus aureus | P38507 (AlphaFold model) |
>5CBN_1 Maltose-binding periplasmic protein (chains B) MGMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV DEALKDAQT
>5CBN_2 mbp3-16,Immunoglobulin G-binding protein A (chains A) SDLGKKLLEAAHAGQDDEVRILMANGADVNAMDNFGVTPLHLAAYWGHFEIVEVLLKYGA DVNASDATGDTPLHLAAKWGYLGIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEI LCKNKAQQAAFYCILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| EYC | 2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid} | C18 H14 Cl2 N2 O8 S2 | 1 |
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 P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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