MolNFT v1 · #144840 · protein
Structure of glycolipid AGSA[16,6P] in complex with mouse CD1D
6C6A: “Structure of glycolipid AGSA[16,6P] in complex with mouse CD1D”. X-ray diffraction, 2 ligands (EL7, NAG). MolNFT v1 #144840 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6C6A
- Type
- protein
- Length
- 369 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0R4J090, P01887
- Ligands
- EL7, NAG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 273 | — | A0A0R4J090 |
| B | — | protein | 96 | — | P01887 |
Ligands and binding sites
- EL7 · N-[(2S,3S,4R)-3,4-dihydroxy-8-oxo-8-[(6-phenylhexyl) amino]-1-{[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy}octan-2-yl]heptadecanamide (non-preferred name) · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A0A0R4J090
- Every structure of UniProt P01887
- Elsewhere: RCSB PDB 6C6A · PDBe 6C6A · UniProt A0A0R4J090 · UniProt P01887
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