Research workbench
Glycosylated form of human LLT1, a ligand for nkr-P1, in this structure forming hexamers
Analyse Glycosylated form of human LLT1, a ligand for nkr-P1, in this structure forming… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QKJ
- Type
- protein
- Length
- 115 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-type lectin domain family 2 member D
- UniProt
- Q9UHP7
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-type lectin domain family 2 member D | protein | 115 | 18% helix, 29% strand | Q9UHP7 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 4QKJ · Glycosylated form of human LLT1, a ligand for NKR-P1, in this structure forming hexamers · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UHP7 · AlphaFold monomer V2.0 prediction for C-type lectin domain family 2 member D (Q9UHP7) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9UHP7
- Elsewhere: RCSB PDB 4QKJ · PDBe 4QKJ · UniProt Q9UHP7
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