MolNFT v1 · #58872 · protein
Hepatoselectivity of statins: design and synthesis of 4-sulfamoyl pyrroles as hmg-CoA reductase inhibitors
3BGL: “Hepatoselectivity of statins: design and synthesis of 4-sulfamoyl pyrroles as hmg-CoA reductase inhibitors”. X-ray diffraction. MolNFT v1 #58872 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BGL
- Type
- protein
- Length
- 1,666 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04035
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 421 | — | P04035 |
| C | — | protein | 414 | — | P04035 |
| D | — | protein | 410 | — | P04035 |
Compared structures
- 3BGL · Hepatoselectivity of Statins: Design and synthesis of 4-sulfamoyl pyrroles as HMG-CoA… · the same entry in another collection · chain A against A, TM-score 1.00
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 P04035
- Elsewhere: RCSB PDB 3BGL · PDBe 3BGL · UniProt P04035
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