Crystal structure of murine class II MHC I-Ab in complex with a human CLIP peptide. Determined by X-ray diffraction at 2.15 Å resolution. Released 18 Feb 2003.
Explore 1MUJ in 3D Show helices and sheets RCSB PDB PDBe
1MUJ contains 16 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.
| 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 | 46-49 | 4 | |
| β-strand | 52-53 | 2 | 2 |
| α-helix | 56-76 | 21 | |
| α-helix | 79-83 | 5 | |
| α-helix | 85-87 | 3 | |
| β-strand | 88-93 | 6 | 3 |
| β-strand | 103-112 | 10 | 3 |
| β-strand | 118-123 | 6 | 4 |
| β-strand | 127 | 1 | 4 |
| β-strand | 132-134 | 3 | 3 |
| α-helix | 137 | 1 | |
| β-strand | 138-139 | 2 | 3 |
| β-strand | 145-153 | 9 | 3 |
| β-strand | 161-166 | 6 | 4 |
| β-strand | 174-178 | 5 | 4 |
| α-helix | 180-182 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 47-48 | 2 | 1 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-62 | 8 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-82 | 2 | |
| α-helix | 83-86 | 5 | |
| α-helix | 87-88 | 2 | |
| α-helix | 90-92 | 3 | |
| β-strand | 95 | 1 | 5 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-103 | 6 | 6 |
| β-strand | 114-122 | 9 | 6 |
| β-strand | 123 | 1 | 5 |
| β-strand | 128-133 | 6 | 7 |
| β-strand | 136-138 | 3 | 7 |
| β-strand | 142-144 | 3 | 6 |
| β-strand | 148-149 | 2 | 6 |
| β-strand | 155-162 | 8 | 6 |
| β-strand | 171-176 | 6 | 7 |
| β-strand | 184-188 | 5 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 89-90 | 2 | 2 |
| α-helix | 96-100 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class II histocompatibility antigen, a-B alpha chain | A | protein | 190 | Mus musculus | P14434 (AlphaFold model) |
| H-2 class II histocompatibility antigen, a beta chain | B | protein | 197 | Mus musculus | P14483 (AlphaFold model) |
| CLIP peptide | C | protein | 36 | Homo sapiens | P04233 (AlphaFold model) |
>1MUJ_1 H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, A-B ALPHA CHAIN (chains A) EDDIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDP QGGLQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPV INITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLK HWSSADLVPR
>1MUJ_2 H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, A BETA CHAIN (chains B) GDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAVTELGRPDAEY WNSQPEILERTRAELDTVCRHNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSV TDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPS LKSPITVEWSSAELVPR
>1MUJ_3 CLIP peptide (chains C) GSHSRGLPKPPKPVSKMRMATPLLMQALPMGSGSGS
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: Prediction of an I-Ab peptide-binding motif. Zhu, Y., Rudensky, A.Y., Teyton, A.L. et al. J Mol Biol (2003) 326:1157-1174. DOI 10.1016/S0022-2836(02)01437-7 · 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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