1F3J: Histocompatibility antigen I-AG7

Histocompatibility antigen I-AG7. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 Sept 2000.

Method
X-ray diffraction
Resolution
3.1 Å
Organisms
Mus musculus, Gallus gallus
Chains
6
Atoms
6,464
Mol. weight
90.62 kDa
Ligands
NAG
Released
20 Sept 2000

Explore 1F3J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F3J contains 18 α-helices and 58 β-strands across 5 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: 3 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand5-15121
β-strand19-2681
β-strand29-3571
β-strand40-4341
α-helix57-7620
α-helix80-845
β-strand88-9362
β-strand103-112102
β-strand118-12363
β-strand126-12723
β-strand132-13432
α-helix135-1373
β-strand138-13922
β-strand145-15392
β-strand161-16663
β-strand174-17853
Chain B: 5 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand7-17111
β-strand24-3291
β-strand35-4171
β-strand47-4931
α-helix55-6410
α-helix68-747
α-helix75-806
α-helix811
α-helix82-866
β-strand9514
β-strand9815
β-strand101-10335
β-strand113-122105
β-strand12314
β-strand128-13366
β-strand136-13726
β-strand142-14545
β-strand148-14925
β-strand155-16395
β-strand170-17676
β-strand184-18966
Chain D: 3 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand5-15127
β-strand19-2687
β-strand29-3577
β-strand40-4347
α-helix57-7620
α-helix80-845
β-strand88-9368
β-strand103-112108
β-strand118-12369
β-strand126-12839
β-strand132-13438
α-helix135-1373
β-strand138-13928
β-strand145-15398
β-strand161-16669
β-strand174-17859
Chain E: 6 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand7-17117
β-strand24-3297
β-strand35-4177
β-strand47-4937
α-helix55-6410
α-helix68-747
α-helix75-806
α-helix811
α-helix82-866
α-helix90-923
β-strand95110
β-strand98-10365
β-strand113-122105
β-strand123110
β-strand128-133611
β-strand136-137211
β-strand142-14545
β-strand148-14925
β-strand155-16395
β-strand170-176711
β-strand184111
β-strand187-189311
Chain Q: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix20-234

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class II histocompatibility antigenA, Dprotein182Mus musculusP04228 (AlphaFold model)
MHC class II nodB, Eprotein187Mus musculusQ31135 (AlphaFold model)
Lysozyme CP, Qprotein14Gallus gallusP00698 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1F3J_1 H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN (chains A, D)
IEADHVGFYGTTVYQSPGDIGQYTHEFDGDELFYVDLDKKKTVWRLPEFGQLILFEPQGG
LQNIAAEKHNLGILTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINI
TWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWE
PE
Sequence of entity 2 (B, E), FASTA
>1F3J_2 MHC CLASS II NOD (chains B, E)
ERHFVHQFKGECYFTNGTQRIRLVTRYIYNREEYLRFDSDVGEYRAVTELGRHSAEYYNK
QYLERTRAELDTACRHNYEETEVPTSLRRLEQPNVAISLSRTEALNHHNTLVCSVTDFYP
AKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPHQGEVYTCHVEHPSLKSPI
TVEWRAQ
Sequence of entity 3 (P, Q), FASTA
>1F3J_3 LYSOZYME C (chains P, Q)
AMKRHGLDNYRGYS

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O66

Primary citation

Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice. Latek, R.R., Suri, A., Petzold, S.J. et al. Immunity (2000) 12:699-710. DOI 10.1016/S1074-7613(00)80220-4 · PubMed

Other PDB entries of the same protein (UniProt P04228 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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