Research workbench
Structure of human NPC1L1 mutant-W347R
Analyse Structure of human NPC1L1 mutant-W347R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N4X
- Type
- protein
- Length
- 953 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of NPC1-like intracellular cholesterol transporter 1
- UniProt
- Q9UHC9
- Ligands
- CLR, NAG
- Pockets
- 9 · best druggability 0.89
Structure
electron microscopy · 1 distinct chain · 55% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of NPC1-like intracellular cholesterol transporter 1 | protein | 953 | 55% helix, 8% strand | Q9UHC9 |
Ligands and binding sites
- CLR · Cholesterol · ligand · 3 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1123 | 0.89 | 0.90 | 109 | CLR |
| 2 | 432 | 0.64 | 0.78 | 39 | empty |
| 3 | 189 | 0.55 | 0.80 | 30 | empty |
| 4 | 93 | 0.41 | 0.78 | 20 | empty |
| 5 | 72 | 0.37 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 7 glycan, 6 disulfide (N-glycosylation, disulfide).
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 Q9UHC9
- Elsewhere: RCSB PDB 7N4X · PDBe 7N4X · UniProt Q9UHC9
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