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
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 12 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 57-76 | 20 | |
| α-helix | 80-84 | 5 | |
| β-strand | 88-93 | 6 | 2 |
| β-strand | 103-112 | 10 | 2 |
| β-strand | 118-123 | 6 | 3 |
| β-strand | 126-127 | 2 | 3 |
| β-strand | 132-134 | 3 | 2 |
| α-helix | 135-137 | 3 | |
| β-strand | 138-139 | 2 | 2 |
| β-strand | 145-153 | 9 | 2 |
| β-strand | 161-166 | 6 | 3 |
| β-strand | 174-178 | 5 | 3 |
Chain B: 5 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-17 | 11 | 1 |
| β-strand | 24-32 | 9 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 55-64 | 10 | |
| α-helix | 68-74 | 7 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81 | 1 | |
| α-helix | 82-86 | 6 | |
| β-strand | 95 | 1 | 4 |
| β-strand | 98 | 1 | 5 |
| β-strand | 101-103 | 3 | 5 |
| β-strand | 113-122 | 10 | 5 |
| β-strand | 123 | 1 | 4 |
| β-strand | 128-133 | 6 | 6 |
| β-strand | 136-137 | 2 | 6 |
| β-strand | 142-145 | 4 | 5 |
| β-strand | 148-149 | 2 | 5 |
| β-strand | 155-163 | 9 | 5 |
| β-strand | 170-176 | 7 | 6 |
| β-strand | 184-189 | 6 | 6 |
Chain D: 3 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-15 | 12 | 7 |
| β-strand | 19-26 | 8 | 7 |
| β-strand | 29-35 | 7 | 7 |
| β-strand | 40-43 | 4 | 7 |
| α-helix | 57-76 | 20 | |
| α-helix | 80-84 | 5 | |
| β-strand | 88-93 | 6 | 8 |
| β-strand | 103-112 | 10 | 8 |
| β-strand | 118-123 | 6 | 9 |
| β-strand | 126-128 | 3 | 9 |
| β-strand | 132-134 | 3 | 8 |
| α-helix | 135-137 | 3 | |
| β-strand | 138-139 | 2 | 8 |
| β-strand | 145-153 | 9 | 8 |
| β-strand | 161-166 | 6 | 9 |
| β-strand | 174-178 | 5 | 9 |
Chain E: 6 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-17 | 11 | 7 |
| β-strand | 24-32 | 9 | 7 |
| β-strand | 35-41 | 7 | 7 |
| β-strand | 47-49 | 3 | 7 |
| α-helix | 55-64 | 10 | |
| α-helix | 68-74 | 7 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81 | 1 | |
| α-helix | 82-86 | 6 | |
| α-helix | 90-92 | 3 | |
| β-strand | 95 | 1 | 10 |
| β-strand | 98-103 | 6 | 5 |
| β-strand | 113-122 | 10 | 5 |
| β-strand | 123 | 1 | 10 |
| β-strand | 128-133 | 6 | 11 |
| β-strand | 136-137 | 2 | 11 |
| β-strand | 142-145 | 4 | 5 |
| β-strand | 148-149 | 2 | 5 |
| β-strand | 155-163 | 9 | 5 |
| β-strand | 170-176 | 7 | 11 |
| β-strand | 184 | 1 | 11 |
| β-strand | 187-189 | 3 | 11 |
Chain Q: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-23 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| H-2 class II histocompatibility antigen | A, D | protein | 182 | Mus musculus | P04228 (AlphaFold model) |
| MHC class II nod | B, E | protein | 187 | Mus musculus | Q31135 (AlphaFold model) |
| Lysozyme C | P, Q | protein | 14 | Gallus gallus | P00698 (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
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
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:
- 6BLQ 1.8 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E
- 7QHP 1.82 Å, Structure of I-Ag7 with a bound hybrid insulin peptide
- 6BLR 1.96 Å, Crystal Structure of IAg7 in complex with insulin mimotope p8E9E6SS
- 6BLX 2.32 Å, Crystal structure of IAg7 in complex with insulin mimotope p8G9E
- 2IAD 2.4 Å, Class II MHC I-ad in complex with an influenza hemagglutinin peptide 126-138
- 5DMK 2.45 Å, Crystal Structure of IAg7 in complex with RLGL-WE14
- 1ES0 2.6 Å, Crystal structure of the murine class II allele I-A(G7) complexed with the glutamic acid…
- 1IAO 2.6 Å, Class II MHC I-ad in complex with ovalbumin peptide 323-339
- 7Z50 2.65 Å, Structure of the highly diabetogenic 4.1-T cell receptor targeting a hybrid insulin…
- 3MBE 2.89 Å, TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)
- 7RDV 2.9 Å, TFH TCR bound to MHC Class II IAd presenting aggrecan epitope
- 3CUP 3.09 Å, Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide…
Browse structure collections
About this viewer
MolViewer shows 1F3J 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.