Structural and kinetic basis for heightened immunogenicity of T cell vaccines. Determined by X-ray diffraction at 1.4 Å resolution. Released 24 May 2005.
Explore 2BNU in 3D Show helices and sheets RCSB PDB PDBe
2BNU contains 11 α-helices and 43 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 | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 30-38 | 9 | 2 |
| β-strand | 44-51 | 8 | 2 |
| β-strand | 56-59 | 4 | 1 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-94 | 9 | 2 |
| β-strand | 103-104 | 2 | 2 |
| β-strand | 108-113 | 6 | 2 |
| α-helix | 114-115 | 2 | |
| β-strand | 122-126 | 5 | 3 |
| β-strand | 135-140 | 6 | 3 |
| β-strand | 157-158 | 2 | 3 |
| α-helix | 159-161 | 3 | |
| β-strand | 162-166 | 5 | 3 |
| α-helix | 167-169 | 3 | |
| β-strand | 171-180 | 10 | 3 |
| α-helix | 187-191 | 5 | |
| β-strand | 201 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 4 |
| β-strand | 9-13 | 5 | 5 |
| β-strand | 18-20 | 3 | 6 |
| β-strand | 21-24 | 4 | 4 |
| β-strand | 30-37 | 8 | 5 |
| β-strand | 41-50 | 10 | 5 |
| β-strand | 53-56 | 4 | 5 |
| β-strand | 64-65 | 2 | 6 |
| β-strand | 72 | 1 | 4 |
| β-strand | 75-77 | 3 | 6 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 5 |
| β-strand | 102-103 | 2 | 5 |
| β-strand | 107-112 | 6 | 5 |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 7 |
| α-helix | 120-121 | 2 | |
| β-strand | 122-126 | 5 | 8 |
| α-helix | 127-129 | 3 | |
| α-helix | 130-136 | 7 | |
| β-strand | 138-148 | 11 | 8 |
| β-strand | 149 | 1 | 7 |
| β-strand | 153-159 | 7 | 9 |
| β-strand | 162-164 | 3 | 9 |
| β-strand | 168-170 | 3 | 8 |
| β-strand | 175-176 | 2 | 8 |
| β-strand | 186-195 | 10 | 8 |
| α-helix | 196-199 | 4 | |
| β-strand | 205-212 | 8 | 9 |
| β-strand | 215 | 1 | 10 |
| β-strand | 229 | 1 | 10 |
| β-strand | 231-238 | 8 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| T-cell receptor alpha chain C region | A | protein | 203 | HOMO SAPIENS | A0A0B4J279 (AlphaFold model), P01848 (AlphaFold model) |
| T-cell receptor beta chain C region | B | protein | 241 | HOMO SAPIENS | A0A0K0K1A5 (AlphaFold model), P01850 (AlphaFold model) |
>2BNU_1 T-CELL RECEPTOR ALPHA CHAIN C REGION (chains A) QEVTQIPAALSVPEGENLVLNCSFTDSAIYNLQWFRQDPGKGLTSLLLIQSSQREQTSGR LNASLDKSSGRSTLYIAASQPGDSATYLCAVRPTSGGSYIPTFGRGTSLIVHPYIQNPDP AVYQLRRSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSN KSDFACANAFNNSIIPEDTFFPS
>2BNU_2 T-CELL RECEPTOR BETA CHAIN C REGION (chains B) GVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGMGLRLIHYSVGAGITDQGEVPN GYNVSRSTTEDFPLRLLSAAPSQTSVYFCASSYVGNTGELFFGEGSRLTVLEDLKNVFPP EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPAL NDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA D
Structural and Kinetic Basis for Heightened Immunogenicity of T Cell Vaccines. Chen, J.-L., Stewart-Jones, G., Bossi, G. et al. J Exp Med (2005) 201:1243. DOI 10.1084/JEM.20042323 · PubMed
Other PDB entries of the same protein (UniProt A0A0B4J279 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2BNU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.