1SEB: HLA class II histocompatibility antigen

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.

Method
X-ray diffraction
Resolution
2.7 Å
Organisms
Homo sapiens, Staphylococcus aureus
Chains
8
Atoms
9,396
Mol. weight
144.65 kDa
Released
20 Jun 1996

Explore 1SEB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and E: 5 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand5-15111
β-strand19-2681
β-strand29-3571
β-strand40-4341
α-helix46-505
β-strand5312
α-helix56-7621
α-helix80-823
β-strand8513
α-helix86-872
β-strand88-9364
β-strand103-112104
β-strand11313
β-strand118-12365
β-strand126-12835
β-strand133-13424
α-helix136-1372
β-strand138-13924
β-strand145-15394
β-strand161-16665
β-strand174-17855
Chains B and F: 5 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand7-18121
β-strand23-3191
β-strand36-4161
β-strand47-4931
α-helix55-617
α-helix65-728
α-helix741
α-helix75-806
α-helix81-866
β-strand9516
β-strand98-10367
β-strand113-122107
β-strand12316
β-strand128-13368
β-strand136-13728
β-strand14417
β-strand148-14927
β-strand155-16397
β-strand170-17678
β-strand184-18968
Chains C and G: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand212
α-helix3-53
α-helix7-126
Chains D and H: 7 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix3-75
α-helix14-163
α-helix22-287
β-strand33-3869
β-strand40-42310
β-strand48-51410
β-strand64-67410
α-helix71-788
β-strand82-8659
β-strand89110
β-strand112-114310
β-strand117-11939
β-strand130111
β-strand150111
β-strand155-156212
α-helix157-17216
β-strand185-190613
β-strand195-199513
α-helix210-2145
α-helix215-2173
β-strand222-223212
β-strand229-234613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
HLA class II histocompatibility antigenA, Eprotein181Homo sapiensP01903 (AlphaFold model)
HLA class II histocompatibility antigenB, Fprotein192Homo sapiensP01911 (AlphaFold model)
Endogenous peptide model, poly-alaC, Gprotein13Homo sapiens
Enterotoxin type BD, Hprotein234Staphylococcus aureusP01552 (AlphaFold model)
Sequence of entity 1 (A, E), FASTA
>1SEB_1 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains A, E)
IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL
ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT
WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF
D
Sequence of entity 2 (B, F), FASTA
>1SEB_2 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains B, F)
GDTRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEY
WNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPSKTQPLQHHNLLVCSVS
GFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSV
TSPLTVEWRARS
Sequence of entity 3 (C, G), FASTA
>1SEB_3 ENDOGENOUS PEPTIDE MODEL, POLY-ALA (chains C, G)
XXXXXXXXXXXXX
Sequence of entity 4 (D, H), FASTA
>1SEB_4 ENTEROTOXIN TYPE B (chains D, H)
SQPDPKPDELHKSSKFTGLMENMKVLYDDNHVSAINVKSIDQFLYFDLIYSIKDTKLGNY
DNVRVEFKNKDLADKYKDKYVDVFGANYYYQCYFSKKTNDINSHQTDKRKTCMYGGVTEH
NGNQLDKYRSITVRVFEDGKNLLSFDVQTNKKKVTAQELDYLTRHYLVKNKKLYEFNNSP
YETGYIKFIENENSFWYDMMPAPGDKFDQSKYLMMYNDNKMVDSKDVKIEVYLT

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 1SEB 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.