Crystal Structure of LILRB2(LIR2/ILT4/CD85d) complexed with HLA-G. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Nov 2006.
Explore 2DYP in 3D Show helices and sheets RCSB PDB PDBe
2DYP contains 15 α-helices and 52 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 | 4-12 | 9 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-53 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 153-161 | 9 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-194 | 9 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 223 | 1 | 4 |
| β-strand | 229-230 | 2 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 3 | 1 | 6 |
| β-strand | 6-11 | 6 | 7 |
| β-strand | 21-30 | 10 | 7 |
| β-strand | 31 | 1 | 6 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 44-46 | 3 | 8 |
| β-strand | 50-51 | 2 | 7 |
| β-strand | 55-56 | 2 | 7 |
| β-strand | 62-70 | 9 | 7 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 91-94 | 4 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| β-strand | 7-11 | 5 | 9 |
| β-strand | 15-17 | 3 | 10 |
| β-strand | 22-27 | 6 | 9 |
| β-strand | 34-39 | 6 | 11 |
| α-helix | 55-57 | 3 | |
| β-strand | 59-62 | 4 | 9 |
| α-helix | 67-69 | 3 | |
| β-strand | 71-79 | 9 | 11 |
| β-strand | 82-83 | 2 | 11 |
| α-helix | 85-89 | 5 | |
| β-strand | 90-92 | 3 | 11 |
| β-strand | 93-95 | 3 | 10 |
| β-strand | 102-106 | 5 | 12 |
| β-strand | 110 | 1 | 13 |
| β-strand | 115-122 | 8 | 12 |
| β-strand | 125 | 1 | 5 |
| β-strand | 129-134 | 6 | 14 |
| β-strand | 142-145 | 4 | 14 |
| β-strand | 155-163 | 9 | 12 |
| β-strand | 170-176 | 7 | 14 |
| β-strand | 183 | 1 | 10 |
| β-strand | 184 | 1 | 14 |
| α-helix | 186-190 | 5 | |
| β-strand | 191-192 | 2 | 14 |
| β-strand | 194 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class I histocompatibility antigen, alpha chain G | A | protein | 277 | Homo sapiens | P17693 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| 9 Mer Peptide From Histone H2A.x | C | protein | 9 | P16104 (AlphaFold model) | |
| Leukocyte immunoglobulin-like receptor subfamily B member 2 | D | protein | 196 | Homo sapiens | Q8N423 (AlphaFold model) |
>2DYP_1 HLA class I histocompatibility antigen, alpha chain G (chains A) MGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSASPRMEPRAPWVEQEGPEY WEEETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYD GKDYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEML QRADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDG TFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRWKQ
>2DYP_2 Beta-2-microglobulin (chains B) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>2DYP_3 9 Mer Peptide From Histone H2A.x (chains C) RIIPRHLQL
>2DYP_4 Leukocyte immunoglobulin-like receptor subfamily B member 2 (chains D) GTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQF RIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQ CESQVAFGGFILCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNS PYVWSSPSDLLELLVP
Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d). Shiroishi, M., Kuroki, K., Rasubala, L. et al. Proc Natl Acad Sci U S A (2006) 103:16412-16417. DOI 10.1073/pnas.0605228103 · PubMed
Other PDB entries of the same protein (UniProt P17693 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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