1LNU: Class II MHC molecule iab

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.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Mus musculus
Chains
8
Atoms
13,265
Mol. weight
184.8 kDa
Ligands
NAG
Released
14 Aug 2002

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

Secondary structure: helices and β-sheets

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.

Chains A, C and E: 4 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand6-15101
β-strand20-2781
β-strand30-3671
β-strand41-4441
α-helix47-526
β-strand5412
α-helix57-7721
α-helix81-855
β-strand91-9443
β-strand104-113103
β-strand118-12474
β-strand133-13533
α-helix136-1383
β-strand139-14023
β-strand146-15493
β-strand162-16874
β-strand175-17954
Chains B, F and H: 10 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand212
α-helix3-75
α-helix9-124
β-strand34-4291
β-strand51-5881
β-strand61-6771
β-strand72-7541
α-helix78-803
α-helix81-899
α-helix91-977
α-helix100-1034
α-helix106-1083
α-helix109-1135
α-helix117-1193
β-strand12215
α-helix123-1242
β-strand125-13176
β-strand141-14996
β-strand15015
β-strand155-16067
β-strand163-16537
β-strand169-17136
β-strand17616
β-strand182-18986
β-strand198-20367
β-strand211-21557
Chain D: 10 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand219
α-helix3-75
α-helix9-124
β-strand34-4298
β-strand51-5888
β-strand61-6778
β-strand72-7548
α-helix78-803
α-helix81-899
α-helix91-977
α-helix100-1034
α-helix106-1083
α-helix109-1135
α-helix117-1193
β-strand122112
α-helix123-1242
β-strand125-131713
β-strand141-149913
β-strand150112
β-strand155-160614
β-strand163-164214
β-strand169-171313
β-strand176113
β-strand182-189813
β-strand198-203614
β-strand211-215514
Chain G: 4 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand6-151021
β-strand20-27821
β-strand30-36721
β-strand41-44421
α-helix47-504
β-strand54122
α-helix57-7721
α-helix81-855
β-strand91-94423
β-strand104-1131023
β-strand118-124724
β-strand133-135323
α-helix136-1383
β-strand139-140223
β-strand146-154923
β-strand162-168724
β-strand175-179524

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class II histocompatibility antigen, A-B alpha chainA, C, E, Gprotein182Mus musculusP14434 (AlphaFold model)
H-2 class II histocompatibility antigen, A beta chainB, D, F, Hprotein217Mus musculusP14483 (AlphaFold model)
Sequence of entity 1 (A, C, E, G), FASTA
>1LNU_1 H-2 class II histocompatibility antigen, A-B alpha chain (chains A, C, E, G)
IEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGG
LQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINI
TWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWE
PE
Sequence of entity 2 (B, D, F, H), FASTA
>1LNU_2 H-2 class II histocompatibility antigen, A beta chain (chains B, D, F, H)
FEAQKAKANKAVDGGGGSLVPRGSGGGGSERHFVYQFMGECYFTNGTQRIRYVTRYIYNR
EEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRR
LEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDW
TFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWKA

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O612

Primary citation

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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