5KSU: HLA-DQ2.5-CLIP1 at 2.73 resolution
Crystal structure of HLA-DQ2.5-CLIP1 at 2.73 resolution. Determined by X-ray diffraction at 2.73 Å resolution. Released 5 Apr 2017.
- Method
- X-ray diffraction
- Resolution
- 2.73 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 6,139
- Mol. weight
- 95.77 kDa
- Released
- 5 Apr 2017
Explore 5KSU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5KSU contains 26 α-helices and 62 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.
Chain A: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-14 | 11 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| α-helix | 36-38 | 3 | |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 46-50 | 5 | |
| β-strand | 52 | 1 | 2 |
| α-helix | 56-76 | 21 | |
| α-helix | 81-87 | 7 | |
| β-strand | 88-93 | 6 | 3 |
| β-strand | 103-112 | 10 | 3 |
| β-strand | 118-123 | 6 | 4 |
| β-strand | 126-128 | 3 | 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 |
Chain B: 8 helices, 15 β-strands
| 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 | 65-71 | 7 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-88 | 8 | |
| α-helix | 90-92 | 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 |
| β-strand | 170-176 | 7 | 7 |
| β-strand | 184-189 | 6 | 7 |
Chain C: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | -1 | 1 | 2 |
Chain D: 4 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-14 | 11 | 8 |
| β-strand | 19-26 | 8 | 8 |
| β-strand | 29-35 | 7 | 8 |
| β-strand | 40-43 | 4 | 8 |
| α-helix | 46-48 | 3 | |
| β-strand | 52 | 1 | 9 |
| α-helix | 57-76 | 20 | |
| α-helix | 81-87 | 7 | |
| β-strand | 88-93 | 6 | 10 |
| β-strand | 103-112 | 10 | 10 |
| β-strand | 118-123 | 6 | 11 |
| β-strand | 126-127 | 2 | 11 |
| β-strand | 132-134 | 3 | 10 |
| α-helix | 137 | 1 | |
| β-strand | 138-139 | 2 | 10 |
| β-strand | 145-153 | 9 | 10 |
| β-strand | 156 | 1 | 12 |
| β-strand | 159 | 1 | 12 |
| β-strand | 161-166 | 6 | 11 |
| β-strand | 174-178 | 5 | 11 |
Chain E: 8 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-18 | 11 | 8 |
| β-strand | 23-32 | 10 | 8 |
| β-strand | 35-41 | 7 | 8 |
| β-strand | 47-49 | 3 | 8 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-63 | 9 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-88 | 8 | |
| α-helix | 90-92 | 3 | |
| β-strand | 95 | 1 | 13 |
| β-strand | 98-103 | 6 | 14 |
| β-strand | 114-122 | 9 | 14 |
| β-strand | 123 | 1 | 13 |
| β-strand | 128-133 | 6 | 15 |
| β-strand | 136-138 | 3 | 15 |
| β-strand | 142-144 | 3 | 14 |
| α-helix | 145-147 | 3 | |
| β-strand | 148-149 | 2 | 14 |
| β-strand | 155-162 | 8 | 14 |
| α-helix | 165-166 | 2 | |
| β-strand | 171-176 | 6 | 15 |
| β-strand | 184-188 | 5 | 15 |
Chain F: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | -1 | 1 | 9 |
| α-helix | 6-9 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| HLA class II histocompatibility antigen, DQ alpha 1 chain | A, D | protein | 199 | Homo sapiens | P01909 (AlphaFold model) |
| MHC class II HLA-DQ-beta-1 | B, E | protein | 204 | Homo sapiens | Q5Y7D3 (AlphaFold model) |
| HLA class II histocompatibility antigen gamma chain | C, F | protein | 15 | Homo sapiens | P04233 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>5KSU_1 HLA class II histocompatibility antigen, DQ alpha 1 chain (chains A, D)
EDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQF
ALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVN
ITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKHW
EPEIPAPMSELTEVDIEGR
Sequence of entity 2 (B, E), FASTA
>5KSU_2 MHC class II HLA-DQ-beta-1 (chains B, E)
RDSPEDFVYQFKGMCYFTNGTERVRLVSRSIYNREEIVRFDSDVGEFRAVTLLGLPAAEY
WNSQKDILERKRAAVDRVCRHNYQLELRTTLQRRVEPTVTISPSRTEALNHHNLLVCSVT
DFYPAQIKVRWFRNDQEETAGVVSTPLIRNGDWTFQILVMLEMTPQRGDVYTCHVEHPSL
QSPITVEWRAQSESAQSKVDIEGR
Sequence of entity 3 (C, F), FASTA
>5KSU_3 HLA class II histocompatibility antigen gamma chain (chains C, F)
PVSKMRMATPLLMQA
Primary citation
Unraveling the structural basis for the unusually rich association of human leukocyte antigen DQ2.5 with class-II-associated invariant chain peptides. Nguyen, T.B., Jayaraman, P., Bergseng, E. et al. J Biol Chem (2017) 292:9218-9228. DOI 10.1074/jbc.M117.785139 · PubMed
Other PDB entries of the same protein (UniProt P01909 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6U3M 1.9 Å, DQ2-P.fluor-alpha1a
- 5KSA 2.0 Å, Bel602-DQ8.5-glia-gamma1 complex
- 6MFG 2.0 Å, HLA-DQ2-glia-alpha1
- 2NNA 2.1 Å, Structure of the MHC class II molecule HLA-DQ8 bound with a deamidated gluten peptide
- 8W84 2.1 Å, HLA-DQ2.5-alpha2 gliadin peptide in complex with DQN0344AE02
- 5KSV 2.19 Å, Crystal structure of HLA-DQ2.5-CLIP2
- 9EJG 2.2 Å, Peptide-independent T cell receptor recognition of HLA-DQ2
- 1S9V 2.22 Å, Crystal structure of HLA-DQ2 complexed with deamidated gliadin peptide
- 8W86 2.24 Å, HLA-DQ2.5-B/C hordein peptide in complex with DQN0385AE02
- 1JK8 2.4 Å, Crystal structure of a human insulin peptide-HLA-DQ8 complex
- 6XP6 2.4 Å, 3C11-DQ2-glia-a2 complex
- 9EJH 2.45 Å, Peptide-independent T cell receptor recognition of HLA-DQ2
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