HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR). Determined by X-ray diffraction at 2.4 Å resolution. Released 17 Aug 2004.
Explore 1T5W in 3D Show helices and sheets RCSB PDB PDBe
1T5W contains 27 α-helices and 66 β-strands across 6 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 | 56-76 | 21 | |
| α-helix | 81-84 | 4 | |
| 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 | 126-128 | 3 | 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 | 7-18 | 12 | 1 |
| β-strand | 23-31 | 9 | 1 |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 47-49 | 3 | 1 |
| β-strand | 51 | 1 | 6 |
| 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 | |
| β-strand | 95 | 1 | 7 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-104 | 7 | 8 |
| β-strand | 113-122 | 10 | 8 |
| β-strand | 123 | 1 | 7 |
| β-strand | 128-133 | 6 | 9 |
| β-strand | 136-137 | 2 | 9 |
| β-strand | 142-144 | 3 | 8 |
| β-strand | 148-149 | 2 | 8 |
| β-strand | 155-163 | 9 | 8 |
| β-strand | 170-176 | 7 | 9 |
| α-helix | 183 | 1 | |
| β-strand | 184-189 | 6 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1 | 1 | 2 |
| α-helix | 5-11 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-18 | 12 | 10 |
| β-strand | 23-31 | 9 | 10 |
| β-strand | 36-41 | 6 | 10 |
| β-strand | 47-49 | 3 | 10 |
| β-strand | 51 | 1 | 6 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-61 | 7 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| α-helix | 87-89 | 3 | |
| β-strand | 95 | 1 | 15 |
| α-helix | 96-97 | 2 | |
| β-strand | 98-104 | 7 | 16 |
| β-strand | 113-122 | 10 | 16 |
| β-strand | 123 | 1 | 15 |
| β-strand | 128-133 | 6 | 17 |
| β-strand | 136-138 | 3 | 17 |
| β-strand | 142-144 | 3 | 16 |
| β-strand | 148-149 | 2 | 16 |
| β-strand | 155-163 | 9 | 16 |
| β-strand | 170-176 | 7 | 17 |
| α-helix | 183 | 1 | |
| β-strand | 184-189 | 6 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1 | 1 | 11 |
| α-helix | 5-9 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class II histocompatibility antigen, DR alpha chain | A, D | protein | 180 | Homo sapiens | P01903 (AlphaFold model) |
| HLA class II histocompatibility antigen, DRB1-1 beta chain | B, E | protein | 190 | Homo sapiens | P01911 (AlphaFold model) |
| 15-mer peptide fragment of Regulatory protein MIG1 | C, F | protein | 15 | P27705 (AlphaFold model) |
>1T5W_1 HLA class II histocompatibility antigen, DR alpha chain (chains A, D) KEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALA NIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTW LRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFD
>1T5W_2 HLA class II histocompatibility antigen, DRB1-1 beta chain (chains B, E) GDTRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEY WNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPSKTQPLQHHNLLVCSVS GFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSV TSPLTVEWRA
>1T5W_3 15-mer peptide fragment of Regulatory protein MIG1 (chains C, F) AAYSDQATPLLLSPR
A Polymorphic Pocket at the P10 Position Contributes to Peptide Binding Specificity in Class II MHC Proteins. Zavala-Ruiz, Z., Strug, I., Anderson, M.W. et al. Chem Biol (2004) 11:1395-1402. DOI 10.1016/j.chembiol.2004.08.007 · 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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