1IAK: Histocompatibility antigen I-ak

Histocompatibility antigen I-ak. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Apr 1998.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Mus musculus
Chains
3
Atoms
3,540
Mol. weight
46.79 kDa
Ligands
NAG
Released
15 Apr 1998

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

Secondary structure: helices and β-sheets

1IAK contains 17 α-helices and 30 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.

Chain A: 4 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand5-15121
β-strand19-2681
β-strand29-3571
β-strand40-4341
α-helix46-505
β-strand5312
α-helix56-7722
α-helix80-845
β-strand88-9363
β-strand103-112103
β-strand118-12364
β-strand126-12724
β-strand132-13433
α-helix1371
β-strand138-13923
β-strand145-15393
β-strand161-16664
β-strand174-17854
Chain B: 12 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand7-18121
α-helix20-223
β-strand23-32101
β-strand35-4171
β-strand47-4931
α-helix52-543
α-helix55-6410
α-helix68-725
α-helix741
α-helix75-806
α-helix81-822
α-helix83-865
α-helix90-923
β-strand9515
α-helix96-972
β-strand98-10366
α-helix106-1072
β-strand113-122106
β-strand12315
β-strand128-13367
β-strand136-13837
β-strand142-14436
α-helix146-1472
β-strand148-14926
β-strand155-16396
β-strand170-17677
β-strand184-18967
Chain P: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand5112
α-helix54-618

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class II I-akAprotein199Mus musculusP01910 (AlphaFold model)
MHC class II I-akBprotein185Mus musculusP06343 (AlphaFold model)
MHC class II I-akPprotein13Mus musculusQ29431 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1IAK_1 MHC CLASS II I-AK (chains A)
EDDIEADHVGSYGITVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFAQLRRFEP
QGGLQNIATGKHNLEILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV
INITWLRNSKSVTDGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK
HWEPEIPAPMSELTETVVC
Sequence of entity 2 (B), FASTA
>1IAK_2 MHC CLASS II I-AK (chains B)
GSFVHQFQPFCYFTNGTQRIRLVIRYIYNREEYVRFDSDVGEYRAVTELGRPDAEYWNKQ
YLERTRAELDTVCRHNYEKTETPTSLRRLEQPSVVISLSRTEALNHHNTLVCSVTDFYPA
KIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLTSPIT
VEWRA
Sequence of entity 3 (P), FASTA
>1IAK_3 MHC CLASS II I-AK (chains P)
STDYGILQINSRW

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63

Primary citation

Crystal structure of I-Ak in complex with a dominant epitope of lysozyme. Fremont, D.H., Monnaie, D., Nelson, C.A. et al. Immunity (1998) 8:305-317. DOI 10.1016/S1074-7613(00)80536-1 · PubMed

Other PDB entries of the same protein (UniProt P01910 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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