Research workbench
Structure of mouse CD1D in complex with C8PHF
Analyse Structure of mouse CD1D in complex with C8PHF in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GMO
- Type
- protein
- Length
- 367 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-cell surface glycoprotein CD1D1; Beta-2 microglobulin
- UniProt
- P11609, Q91XJ8
- Ligands
- C8F, PLM, NAG, MAN, BMA, FUC
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-cell surface glycoprotein CD1D1 | protein | 268 | 27% helix, 41% strand | P11609 |
| B | Beta-2 microglobulin | protein | 99 | 0% helix, 49% strand | Q91XJ8 |
Ligands and binding sites
- C8F · 8-(4-fluorophenyl)-N-{(1S,2S,3R)-1-[(alpha-D-galactopyranosyloxy)methyl]-2,3-dihydroxyheptadecyl}octanamide · ligand · chains A
- PLM · Palmitic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 4 copies
- BMA · beta-D-mannopyranose · sugar · 2 copies
- FUC · alpha-L-fucopyranose · sugar · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 667 | 0.85 | 0.88 | 61 | C8F, PLM |
| 2 | 505 | 0.66 | 0.78 | 55 | EDO |
| 3 | 185 | 0.45 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1199 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P11609
- Every structure of UniProt Q91XJ8
- Elsewhere: RCSB PDB 3GMO · PDBe 3GMO · UniProt P11609 · UniProt Q91XJ8
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