HLA-DR1 with covalently linked CLIP106-120 in canonical orientation. Determined by X-ray diffraction at 2.36 Å resolution. Released 1 Aug 2012.
Explore 4AH2 in 3D Show helices and sheets RCSB PDB PDBe
4AH2 contains 15 α-helices and 32 β-strands across 2 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 | 11 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 46-50 | 5 | |
| β-strand | 53 | 1 | 2 |
| α-helix | 57-76 | 20 | |
| α-helix | 80-84 | 5 | |
| β-strand | 85 | 1 | 3 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-93 | 6 | 4 |
| β-strand | 103-112 | 10 | 4 |
| β-strand | 113 | 1 | 3 |
| β-strand | 118-123 | 6 | 5 |
| β-strand | 126-127 | 2 | 5 |
| β-strand | 133-134 | 2 | 4 |
| α-helix | 137 | 1 | |
| β-strand | 138-139 | 2 | 4 |
| β-strand | 145-153 | 9 | 4 |
| β-strand | 160-166 | 7 | 5 |
| β-strand | 174-179 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -29 | 1 | 2 |
| α-helix | -28--27 | 2 | |
| α-helix | -23--18 | 6 | |
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-62 | 8 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-89 | 3 | |
| β-strand | 95 | 1 | 6 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-103 | 6 | 7 |
| β-strand | 113-122 | 10 | 7 |
| β-strand | 123 | 1 | 6 |
| β-strand | 128-133 | 6 | 8 |
| β-strand | 136-137 | 2 | 8 |
| β-strand | 142-144 | 3 | 7 |
| β-strand | 148-149 | 2 | 7 |
| β-strand | 155-163 | 9 | 7 |
| β-strand | 171-176 | 6 | 8 |
| α-helix | 183 | 1 | |
| β-strand | 184-188 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class II histocompatibility antigen, dr alpha chain | A | protein | 193 | HOMO SAPIENS | P01903 (AlphaFold model) |
| HLA class II histocompatibility antigen gamma chain, HLA class II histocompatibility… | B | protein | 229 | HOMO SAPIENS | P01911 (AlphaFold model), P04233 (AlphaFold model) |
>4AH2_1 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN (chains A) MIKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGA LANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNV TWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWE FDAPSPLPETTEN
>4AH2_2 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN\,DRB1-1 BETA CHAIN (chains B) MKMRMATPLLMQALPMGGGGSGGGGSGGGGSGDTRPRFLWQLKFECHFFNGTERVRLLER CIYNQEESVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTYCRHNYGVGESF TVQRRVEPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQ NGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSK
Peptide Linkage to the Alpha-Subunit of Mhcii Creates a Stably Inverted Antigen Presentation Complex. Schlundt, A., Gunther, S., Sticht, J. et al. J Mol Biol (2012) 423:294. DOI 10.1016/J.JMB.2012.07.008 · PubMed
Other PDB entries of the same protein (UniProt P01903 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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