Structure of a monoclonal antibody complexed with its MHC-I antigen. Determined by X-ray diffraction at 1.7 Å resolution. Released 25 Jul 2012.
Explore 3UYR in 3D Show helices and sheets RCSB PDB PDBe
3UYR contains 20 α-helices and 44 β-strands across 3 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 | 4-6 | 3 | 1 |
| α-helix | 7-8 | 2 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-24 | 7 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 2 |
| β-strand | 44-51 | 8 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 2 |
| β-strand | 103-107 | 5 | 2 |
| β-strand | 111-115 | 5 | 2 |
| α-helix | 119-120 | 2 | |
| β-strand | 121 | 1 | 3 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 4 |
| β-strand | 139-149 | 11 | 4 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155-158 | 4 | 5 |
| α-helix | 159-161 | 3 | |
| β-strand | 163 | 1 | 5 |
| β-strand | 167-175 | 9 | 4 |
| β-strand | 178-188 | 11 | 4 |
| α-helix | 189-191 | 3 | |
| β-strand | 198-203 | 6 | 5 |
| α-helix | 204-206 | 3 | |
| β-strand | 208-213 | 6 | 5 |
| α-helix | 214 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-14 | 5 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 30 | 1 | 8 |
| β-strand | 36 | 1 | 8 |
| β-strand | 38-43 | 6 | 7 |
| β-strand | 49-54 | 6 | 7 |
| β-strand | 58-59 | 2 | 7 |
| α-helix | 60 | 1 | |
| β-strand | 67-72 | 6 | 6 |
| β-strand | 75-80 | 6 | 6 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-95 | 7 | 7 |
| β-strand | 101-102 | 2 | 7 |
| β-strand | 106-111 | 6 | 7 |
| β-strand | 115 | 1 | 9 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 10 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-129 | 4 | |
| β-strand | 133-143 | 11 | 10 |
| β-strand | 144 | 1 | 9 |
| β-strand | 149-154 | 6 | 11 |
| β-strand | 157-158 | 2 | 11 |
| β-strand | 163-167 | 5 | 10 |
| α-helix | 168-171 | 4 | |
| β-strand | 177-186 | 10 | 10 |
| α-helix | 187-190 | 4 | |
| β-strand | 195-201 | 7 | 11 |
| α-helix | 208 | 1 | |
| β-strand | 209-214 | 6 | 11 |
| α-helix | 215-217 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 50-52 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| antibody Fab heavy chain | H | protein | 216 | Mus musculus | |
| antibody Fab light chain | L | protein | 218 | Mus musculus | A2NHM3 (AlphaFold model) |
| H-2 class I histocompatibility antigen, L-D alpha chain | P | protein | 8 | Mus musculus | P01897 (AlphaFold model) |
>3UYR_1 antibody Fab heavy chain (chains H) EVKLVESEGGLVQPGSSMKLSCTASGFTFSDYYMAWVRQVPEKGLEWVANINYDGSSTYY LDSLKGRFIISRDIAKNILYLQMSSLRCEDTATYYCARLTNGYLDVWGAGTTVTVSSAKT TPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLESGLYT MSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEP
>3UYR_2 antibody Fab light chain (chains L) DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPNLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPTFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>3UYR_3 H-2 class I histocompatibility antigen, L-D alpha chain (chains P) EPQAPWME
The Peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics. Mage, M.G., Dolan, M.A., Wang, R. et al. J Immunol (2012) 189:1391-1399. DOI 10.4049/jimmunol.1200831 · PubMed
Other PDB entries of the same protein (UniProt A2NHM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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