A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Mar 2006.
Explore 2EYR in 3D Show helices and sheets RCSB PDB PDBe
2EYR contains 12 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 | 3-6 | 4 | 1 |
| β-strand | 9-13 | 5 | 2 |
| β-strand | 18-24 | 7 | 1 |
| β-strand | 31-37 | 7 | 2 |
| β-strand | 44-50 | 7 | 2 |
| β-strand | 55-58 | 4 | 1 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 2 |
| β-strand | 104-106 | 3 | 2 |
| β-strand | 110-115 | 6 | 2 |
| β-strand | 124-128 | 5 | 3 |
| β-strand | 137-142 | 6 | 3 |
| α-helix | 151-153 | 3 | |
| β-strand | 158-160 | 3 | 3 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-168 | 5 | 3 |
| β-strand | 173-182 | 10 | 3 |
| β-strand | 203 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 4 |
| β-strand | 10-14 | 5 | 5 |
| β-strand | 19-21 | 3 | 6 |
| β-strand | 22-25 | 4 | 4 |
| β-strand | 31-37 | 7 | 5 |
| α-helix | 42-43 | 2 | |
| β-strand | 44-49 | 6 | 5 |
| β-strand | 56-57 | 2 | 5 |
| β-strand | 65-67 | 3 | 6 |
| β-strand | 74 | 1 | 4 |
| β-strand | 77-79 | 3 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 5 |
| β-strand | 106-108 | 3 | 5 |
| β-strand | 112-117 | 6 | 5 |
| α-helix | 120-122 | 3 | |
| β-strand | 124 | 1 | 7 |
| α-helix | 125-126 | 2 | |
| β-strand | 127-131 | 5 | 8 |
| α-helix | 132-134 | 3 | |
| α-helix | 135-141 | 7 | |
| β-strand | 143-153 | 11 | 8 |
| β-strand | 154 | 1 | 7 |
| β-strand | 158-164 | 7 | 9 |
| β-strand | 167-169 | 3 | 9 |
| β-strand | 173-175 | 3 | 8 |
| α-helix | 179 | 1 | |
| β-strand | 180-181 | 2 | 8 |
| β-strand | 191-200 | 10 | 8 |
| α-helix | 201-205 | 5 | |
| β-strand | 210-217 | 8 | 9 |
| β-strand | 220 | 1 | 10 |
| α-helix | 231-232 | 2 | |
| β-strand | 234 | 1 | 10 |
| β-strand | 236-243 | 8 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NKT12 | A | protein | 210 | Homo sapiens | P01848 (AlphaFold model) |
| NKT12 | B | protein | 241 | Homo sapiens | A0A5B9 (AlphaFold model) |
>2EYR_1 NKT12 (chains A) HMKNQVEQSPQSLIILEGKNCTLQCNYTVSPFSNLRWYKQDTGRGPVSLTIMTFSENTKS NGRYTATLDADTKQSSLHITASQLSDSASYICVVSDRGSTLGRLYFGRGTQLTVWPDIQN PDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVA WSNKSDFACANAFNNSIIPEDTFFPSPESS
>2EYR_2 NKT12 (chains B) DIYQTPRYLVIGTGKKITLECSQTMGHDKMYWYQQDPGMELHLIHYSYGVNSTEKGDLSS ESTVSRIRTEHFPLTLESARPSHTSQYLCASTSRRGSYEQYFGPGTRLTVTEDLKNVFPP EVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPAL NDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA D
A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d/glycolipid recognition. Kjer-Nielsen, L., Borg, N.A., Pellicci, D.G. et al. J Exp Med (2006) 203:661-673. DOI 10.1084/jem.20051777 · PubMed
Other PDB entries of the same protein (UniProt P01848 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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