Crystal structure of class II MHC molecule iab bound to EALPHA3K peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Aug 2002.
Explore 1LNU in 3D Show helices and sheets RCSB PDB PDBe
1LNU contains 56 α-helices and 116 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 | 6-15 | 10 | 1 |
| β-strand | 20-27 | 8 | 1 |
| β-strand | 30-36 | 7 | 1 |
| β-strand | 41-44 | 4 | 1 |
| α-helix | 47-52 | 6 | |
| β-strand | 54 | 1 | 2 |
| α-helix | 57-77 | 21 | |
| α-helix | 81-85 | 5 | |
| β-strand | 91-94 | 4 | 3 |
| β-strand | 104-113 | 10 | 3 |
| β-strand | 118-124 | 7 | 4 |
| β-strand | 133-135 | 3 | 3 |
| α-helix | 136-138 | 3 | |
| β-strand | 139-140 | 2 | 3 |
| β-strand | 146-154 | 9 | 3 |
| β-strand | 162-168 | 7 | 4 |
| β-strand | 175-179 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| α-helix | 3-7 | 5 | |
| α-helix | 9-12 | 4 | |
| β-strand | 34-42 | 9 | 1 |
| β-strand | 51-58 | 8 | 1 |
| β-strand | 61-67 | 7 | 1 |
| β-strand | 72-75 | 4 | 1 |
| α-helix | 78-80 | 3 | |
| α-helix | 81-89 | 9 | |
| α-helix | 91-97 | 7 | |
| α-helix | 100-103 | 4 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-113 | 5 | |
| α-helix | 117-119 | 3 | |
| β-strand | 122 | 1 | 5 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-131 | 7 | 6 |
| β-strand | 141-149 | 9 | 6 |
| β-strand | 150 | 1 | 5 |
| β-strand | 155-160 | 6 | 7 |
| β-strand | 163-165 | 3 | 7 |
| β-strand | 169-171 | 3 | 6 |
| β-strand | 176 | 1 | 6 |
| β-strand | 182-189 | 8 | 6 |
| β-strand | 198-203 | 6 | 7 |
| β-strand | 211-215 | 5 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 9 |
| α-helix | 3-7 | 5 | |
| α-helix | 9-12 | 4 | |
| β-strand | 34-42 | 9 | 8 |
| β-strand | 51-58 | 8 | 8 |
| β-strand | 61-67 | 7 | 8 |
| β-strand | 72-75 | 4 | 8 |
| α-helix | 78-80 | 3 | |
| α-helix | 81-89 | 9 | |
| α-helix | 91-97 | 7 | |
| α-helix | 100-103 | 4 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-113 | 5 | |
| α-helix | 117-119 | 3 | |
| β-strand | 122 | 1 | 12 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-131 | 7 | 13 |
| β-strand | 141-149 | 9 | 13 |
| β-strand | 150 | 1 | 12 |
| β-strand | 155-160 | 6 | 14 |
| β-strand | 163-164 | 2 | 14 |
| β-strand | 169-171 | 3 | 13 |
| β-strand | 176 | 1 | 13 |
| β-strand | 182-189 | 8 | 13 |
| β-strand | 198-203 | 6 | 14 |
| β-strand | 211-215 | 5 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-15 | 10 | 21 |
| β-strand | 20-27 | 8 | 21 |
| β-strand | 30-36 | 7 | 21 |
| β-strand | 41-44 | 4 | 21 |
| α-helix | 47-50 | 4 | |
| β-strand | 54 | 1 | 22 |
| α-helix | 57-77 | 21 | |
| α-helix | 81-85 | 5 | |
| β-strand | 91-94 | 4 | 23 |
| β-strand | 104-113 | 10 | 23 |
| β-strand | 118-124 | 7 | 24 |
| β-strand | 133-135 | 3 | 23 |
| α-helix | 136-138 | 3 | |
| β-strand | 139-140 | 2 | 23 |
| β-strand | 146-154 | 9 | 23 |
| β-strand | 162-168 | 7 | 24 |
| β-strand | 175-179 | 5 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class II histocompatibility antigen, A-B alpha chain | A, C, E, G | protein | 182 | Mus musculus | P14434 (AlphaFold model) |
| H-2 class II histocompatibility antigen, A beta chain | B, D, F, H | protein | 217 | Mus musculus | P14483 (AlphaFold model) |
>1LNU_1 H-2 class II histocompatibility antigen, A-B alpha chain (chains A, C, E, G) IEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGG LQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINI TWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWE PE
>1LNU_2 H-2 class II histocompatibility antigen, A beta chain (chains B, D, F, H) FEAQKAKANKAVDGGGGSLVPRGSGGGGSERHFVYQFMGECYFTNGTQRIRYVTRYIYNR EEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRR LEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDW TFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWKA
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 12 |
Alternate interactions define the binding of peptides to the MHC molecule IA(b). Liu, X., Dai, S., Crawford, F. et al. Proc Natl Acad Sci U S A (2002) 99:8820-8825. DOI 10.1073/pnas.132272099 · PubMed
Other PDB entries of the same protein (UniProt P14434 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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