MolNFT v1 · #104765 · protein
Dimeric form of human LLT1, a ligand for nkr-P1
4QKI · C-type lectin domain family 2 member D: “Dimeric form of human LLT1, a ligand for nkr-P1”. X-ray diffraction, 1 ligand (NAG), 1 pocket (best druggability 0.70). MolNFT v1 #104765 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4QKI
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- 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
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-type lectin domain family 2 member D | protein | 122 | 16% helix, 30% strand | Q9UHP7 |
| B | C-type lectin domain family 2 member D | protein | 120 | 18% helix, 31% strand | Q9UHP7 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.70 | 0.94 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 791 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 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 Q9UHP7
- Elsewhere: RCSB PDB 4QKI · PDBe 4QKI · UniProt Q9UHP7
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