9RSE: Human CD1d with lipid antigen bound

Human CD1d with lipid antigen bound. Determined by X-ray diffraction at 1.76 Å resolution. Released 15 Jul 2026.

Method
X-ray diffraction
Resolution
1.76 Å
Organism
Homo sapiens
Chains
4
Atoms
7,207
Mol. weight
92.92 kDa
Ligands
AGH
Released
15 Jul 2026

Explore 9RSE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 13 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand10-20111
β-strand23-32101
β-strand35-4061
α-helix471
β-strand48-4921
α-helix60-8829
α-helix90-912
α-helix931
β-strand94-105121
β-strand109-118101
β-strand121-12771
β-strand130-13341
α-helix141-1499
α-helix152-1609
α-helix161-1655
α-helix166-17611
α-helix178-1814
β-strand18512
α-helix186-1872
β-strand188-19473
β-strand201-211113
β-strand21212
β-strand217-22264
β-strand225-22624
β-strand231-23223
β-strand236-23723
α-helix2381
β-strand243-252103
α-helix253-2553
β-strand260-26454
α-helix266-2683
β-strand273-27644
Chain B: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand415
α-helix5-62
β-strand7-1266
β-strand22-31106
β-strand3215
β-strand36-4277
β-strand45-4627
β-strand51-5226
α-helix53-553
β-strand56-5726
β-strand63-7196
β-strand79-8577
β-strand92-9547
Chain C: 13 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand10-20118
β-strand23-32108
β-strand35-4068
α-helix471
β-strand48-4928
α-helix60-8829
α-helix90-912
α-helix931
β-strand94-104118
α-helix106-1083
β-strand110-11898
β-strand121-12778
β-strand130-13348
α-helix140-14910
α-helix152-1609
α-helix161-1655
α-helix166-17611
α-helix178-1825
β-strand18519
α-helix186-1872
β-strand188-193610
β-strand201-2111110
β-strand21219
β-strand217-222611
β-strand225-226211
β-strand231-232210
β-strand236-237210
β-strand243-2521010
α-helix253-2553
β-strand259-264611
α-helix266-2683
β-strand273-276411
Chain D: 3 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand4112
α-helix5-62
β-strand7-12613
β-strand22-311013
β-strand32112
β-strand36-42714
β-strand45-46214
α-helix471
β-strand51-52213
α-helix53-553
β-strand56-57213
β-strand63-71913
β-strand79-85714
β-strand92-95414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Antigen-presenting glycoprotein CD1dA, Cprotein296Homo sapiensP15813 (AlphaFold model)
Beta-2-microglobulinB, Dprotein100Homo sapiensP61769 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>9RSE_1 Antigen-presenting glycoprotein CD1d (chains A, C)
MVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSNDSDTVRSLKPWSQGTFSDQ
QWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGCEVHPGNASNNFFHVAFQGK
DILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLLNGTCPQFVSGLLESGKSEL
KKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMRGEQEQQGTQPGDILPNADE
TWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGPGSGGGLNDIFEAQKIEWH
Sequence of entity 2 (B, D), FASTA
>9RSE_2 Beta-2-microglobulin (chains B, D)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM

Ligands and cofactors

IDNameFormulaCopies
AGHN-{(1S,2R,3S)-1-[(alpha-D-galactopyranosyloxy)methyl]-2,3-dihydroxyheptadecyl}h…C50 H99 N O92

Water and common crystallization additives (1PE) are not listed.

Primary citation

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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