Human CD1d with lipid antigen bound. Determined by X-ray diffraction at 1.76 Å resolution. Released 15 Jul 2026.
Explore 9RSE in 3D Show helices and sheets RCSB PDB PDBe
9RSE contains 31 α-helices and 60 β-strands across 4 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 | 10-20 | 11 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-40 | 6 | 1 |
| α-helix | 47 | 1 | |
| β-strand | 48-49 | 2 | 1 |
| α-helix | 60-88 | 29 | |
| α-helix | 90-91 | 2 | |
| α-helix | 93 | 1 | |
| β-strand | 94-105 | 12 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-127 | 7 | 1 |
| β-strand | 130-133 | 4 | 1 |
| α-helix | 141-149 | 9 | |
| α-helix | 152-160 | 9 | |
| α-helix | 161-165 | 5 | |
| α-helix | 166-176 | 11 | |
| α-helix | 178-181 | 4 | |
| β-strand | 185 | 1 | 2 |
| α-helix | 186-187 | 2 | |
| β-strand | 188-194 | 7 | 3 |
| β-strand | 201-211 | 11 | 3 |
| β-strand | 212 | 1 | 2 |
| β-strand | 217-222 | 6 | 4 |
| β-strand | 225-226 | 2 | 4 |
| β-strand | 231-232 | 2 | 3 |
| β-strand | 236-237 | 2 | 3 |
| α-helix | 238 | 1 | |
| β-strand | 243-252 | 10 | 3 |
| α-helix | 253-255 | 3 | |
| β-strand | 260-264 | 5 | 4 |
| α-helix | 266-268 | 3 | |
| β-strand | 273-276 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 5 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 6 |
| β-strand | 22-31 | 10 | 6 |
| β-strand | 32 | 1 | 5 |
| β-strand | 36-42 | 7 | 7 |
| β-strand | 45-46 | 2 | 7 |
| β-strand | 51-52 | 2 | 6 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 6 |
| β-strand | 63-71 | 9 | 6 |
| β-strand | 79-85 | 7 | 7 |
| β-strand | 92-95 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-20 | 11 | 8 |
| β-strand | 23-32 | 10 | 8 |
| β-strand | 35-40 | 6 | 8 |
| α-helix | 47 | 1 | |
| β-strand | 48-49 | 2 | 8 |
| α-helix | 60-88 | 29 | |
| α-helix | 90-91 | 2 | |
| α-helix | 93 | 1 | |
| β-strand | 94-104 | 11 | 8 |
| α-helix | 106-108 | 3 | |
| β-strand | 110-118 | 9 | 8 |
| β-strand | 121-127 | 7 | 8 |
| β-strand | 130-133 | 4 | 8 |
| α-helix | 140-149 | 10 | |
| α-helix | 152-160 | 9 | |
| α-helix | 161-165 | 5 | |
| α-helix | 166-176 | 11 | |
| α-helix | 178-182 | 5 | |
| β-strand | 185 | 1 | 9 |
| α-helix | 186-187 | 2 | |
| β-strand | 188-193 | 6 | 10 |
| β-strand | 201-211 | 11 | 10 |
| β-strand | 212 | 1 | 9 |
| β-strand | 217-222 | 6 | 11 |
| β-strand | 225-226 | 2 | 11 |
| β-strand | 231-232 | 2 | 10 |
| β-strand | 236-237 | 2 | 10 |
| β-strand | 243-252 | 10 | 10 |
| α-helix | 253-255 | 3 | |
| β-strand | 259-264 | 6 | 11 |
| α-helix | 266-268 | 3 | |
| β-strand | 273-276 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 12 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 13 |
| β-strand | 22-31 | 10 | 13 |
| β-strand | 32 | 1 | 12 |
| β-strand | 36-42 | 7 | 14 |
| β-strand | 45-46 | 2 | 14 |
| α-helix | 47 | 1 | |
| β-strand | 51-52 | 2 | 13 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 13 |
| β-strand | 63-71 | 9 | 13 |
| β-strand | 79-85 | 7 | 14 |
| β-strand | 92-95 | 4 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antigen-presenting glycoprotein CD1d | A, C | protein | 296 | Homo sapiens | P15813 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
>9RSE_1 Antigen-presenting glycoprotein CD1d (chains A, C) MVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSNDSDTVRSLKPWSQGTFSDQ QWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGCEVHPGNASNNFFHVAFQGK DILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLLNGTCPQFVSGLLESGKSEL KKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMRGEQEQQGTQPGDILPNADE TWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGPGSGGGLNDIFEAQKIEWH
>9RSE_2 Beta-2-microglobulin (chains B, D) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
| ID | Name | Formula | Copies |
|---|---|---|---|
| AGH | N-{(1S,2R,3S)-1-[(alpha-D-galactopyranosyloxy)methyl]-2,3-dihydroxyheptadecyl}h… | C50 H99 N O9 | 2 |
Water and common crystallization additives (1PE) are not listed.
Structural features of human and macaque CD1d: Implications for antigen presentation. Burns, D., Look, A., Turner, S. et al. To be published.
Other PDB entries of the same protein (UniProt P15813 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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