Complex of the human MHC class II glycoprotein HLA-DR1 and the bacterial superantigen seb. Determined by X-ray diffraction at 2.7 Å resolution. Released 20 Jun 1996.
Explore 1SEB in 3D Show helices and sheets RCSB PDB PDBe
1SEB contains 38 α-helices and 94 β-strands across 8 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 | 5-15 | 11 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 46-50 | 5 | |
| β-strand | 53 | 1 | 2 |
| α-helix | 56-76 | 21 | |
| α-helix | 80-82 | 3 | |
| β-strand | 85 | 1 | 3 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-93 | 6 | 4 |
| β-strand | 103-112 | 10 | 4 |
| β-strand | 113 | 1 | 3 |
| β-strand | 118-123 | 6 | 5 |
| β-strand | 126-128 | 3 | 5 |
| β-strand | 133-134 | 2 | 4 |
| α-helix | 136-137 | 2 | |
| β-strand | 138-139 | 2 | 4 |
| β-strand | 145-153 | 9 | 4 |
| β-strand | 161-166 | 6 | 5 |
| β-strand | 174-178 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-31 | 9 | 1 |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 55-61 | 7 | |
| α-helix | 65-72 | 8 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| β-strand | 95 | 1 | 6 |
| β-strand | 98-103 | 6 | 7 |
| β-strand | 113-122 | 10 | 7 |
| β-strand | 123 | 1 | 6 |
| β-strand | 128-133 | 6 | 8 |
| β-strand | 136-137 | 2 | 8 |
| β-strand | 144 | 1 | 7 |
| β-strand | 148-149 | 2 | 7 |
| β-strand | 155-163 | 9 | 7 |
| β-strand | 170-176 | 7 | 8 |
| β-strand | 184-189 | 6 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| α-helix | 3-5 | 3 | |
| α-helix | 7-12 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-7 | 5 | |
| α-helix | 14-16 | 3 | |
| α-helix | 22-28 | 7 | |
| β-strand | 33-38 | 6 | 9 |
| β-strand | 40-42 | 3 | 10 |
| β-strand | 48-51 | 4 | 10 |
| β-strand | 64-67 | 4 | 10 |
| α-helix | 71-78 | 8 | |
| β-strand | 82-86 | 5 | 9 |
| β-strand | 89 | 1 | 10 |
| β-strand | 112-114 | 3 | 10 |
| β-strand | 117-119 | 3 | 9 |
| β-strand | 130 | 1 | 11 |
| β-strand | 150 | 1 | 11 |
| β-strand | 155-156 | 2 | 12 |
| α-helix | 157-172 | 16 | |
| β-strand | 185-190 | 6 | 13 |
| β-strand | 195-199 | 5 | 13 |
| α-helix | 210-214 | 5 | |
| α-helix | 215-217 | 3 | |
| β-strand | 222-223 | 2 | 12 |
| β-strand | 229-234 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class II histocompatibility antigen | A, E | protein | 181 | Homo sapiens | P01903 (AlphaFold model) |
| HLA class II histocompatibility antigen | B, F | protein | 192 | Homo sapiens | P01911 (AlphaFold model) |
| Endogenous peptide model, poly-ala | C, G | protein | 13 | Homo sapiens | |
| Enterotoxin type B | D, H | protein | 234 | Staphylococcus aureus | P01552 (AlphaFold model) |
>1SEB_1 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains A, E) IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF D
>1SEB_2 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains B, F) GDTRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEY WNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPSKTQPLQHHNLLVCSVS GFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSV TSPLTVEWRARS
>1SEB_3 ENDOGENOUS PEPTIDE MODEL, POLY-ALA (chains C, G) XXXXXXXXXXXXX
>1SEB_4 ENTEROTOXIN TYPE B (chains D, H) SQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNY DNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEH NGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSP YETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLT
Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Jardetzky, T.S., Brown, J.H., Gorga, J.C. et al. Nature (1994) 368:711-718. DOI 10.1038/368711a0 · PubMed
Other PDB entries of the same protein (UniProt P01903 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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