Crystal structure of HLA-DQ0602 in complex with a hypocretin peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Feb 2004.
Explore 1UVQ in 3D Show helices and sheets RCSB PDB PDBe
1UVQ 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 | 7-17 | 11 | 1 |
| β-strand | 22-29 | 8 | 1 |
| β-strand | 32-38 | 7 | 1 |
| β-strand | 43-45 | 3 | 1 |
| α-helix | 49-54 | 6 | |
| β-strand | 56 | 1 | 2 |
| α-helix | 59-79 | 21 | |
| α-helix | 84-86 | 3 | |
| α-helix | 88-90 | 3 | |
| β-strand | 91-96 | 6 | 3 |
| β-strand | 106-115 | 10 | 3 |
| β-strand | 121-126 | 6 | 4 |
| β-strand | 129-131 | 3 | 4 |
| β-strand | 135-137 | 3 | 3 |
| β-strand | 141-142 | 2 | 3 |
| β-strand | 148-156 | 9 | 3 |
| β-strand | 164-169 | 6 | 4 |
| β-strand | 177-180 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-18 | 11 | 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 | 81-82 | 2 | |
| α-helix | 83-87 | 5 | |
| α-helix | 88-90 | 3 | |
| β-strand | 95 | 1 | 5 |
| 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 |
| α-helix | 145-147 | 3 | |
| β-strand | 148-149 | 2 | 6 |
| β-strand | 155-162 | 8 | 6 |
| α-helix | 163-164 | 2 | |
| β-strand | 171-176 | 6 | 7 |
| β-strand | 184-188 | 5 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| α-helix | 3-4 | 2 | |
| α-helix | 6-9 | 4 | |
| α-helix | 11-12 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class II histocompatibility antigen | A | protein | 197 | HOMO SAPIENS | E9PMV2 (AlphaFold model) |
| HLA class II histocompatibility antigen | B | protein | 198 | HOMO SAPIENS | P01920 (AlphaFold model) |
| Orexin | C | protein | 33 | HOMO SAPIENS | O43612 (AlphaFold model) |
>1UVQ_1 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains A) EDIVADHVASCGVNLYQFYGPSGQYTHEFDGDEQFYVDLERKETAWRWPEFSKFGGFDPQ GALRNMAVAKHNLNIMIKRYNSTAATNEVPEVTVFSKSPVTLGQPNTLICLVDNIFPPVV NITWLSNGQSVTEGVSETSFLSKSDHSFFKISYLTFLPSADEIYDCKVEHWGLDQPLLKH WEPEIPAPMSELTETVD
>1UVQ_2 HLA CLASS II HISTOCOMPATIBILITY ANTIGEN (chains B) SPEDFVFQFKGMCYFTNGTERVRLVTRYIYNREEYARFDSDVGVYRAVTPQGRPDAEYWN SQKEVLEGTRAELDTVCRHNYEVAFRGILQRRVEPTVTISPSRTEALNHHNLLVCSVTDF YPGQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQILVMLEMTPQRGDVYTCHVEHPSLQS PITVEWRAQSESAQSKVD
>1UVQ_3 OREXIN (chains C) EGRDSMNLPSTKVSWAAVGGGGSLVPRGSGGGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| GLY | Glycine | C2 H5 N O2 | 1 |
Water and common crystallization additives (ACY) are not listed.
Crystal Structure of Hla-Dq0602 that Protects Against Type 1 Diabetes and Confers Strong Susceptibility to Narcolepsy. Siebold, C., Hansen, B.E., Wyer, J.R. et al. Proc Natl Acad Sci U S A (2004) 101:1999. DOI 10.1073/PNAS.0308458100 · PubMed
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