Research workbench
P-glycoprotein mutant-Y306A and C952A-with BDE100
Analyse P-glycoprotein mutant-Y306A and C952A-with BDE100 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UJW
- Type
- protein
- Length
- 1,182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P21447
- Ligands
- 4C8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1182 | — | P21447 |
Ligands and binding sites
- 4C8 · 2,4-dibromophenyl 2,4,6-tribromophenyl ether · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UJW · P-glycoprotein mutant-Y306A and C952A-with BDE100 · 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 P21447
- Elsewhere: RCSB PDB 6UJW · PDBe 6UJW · UniProt P21447
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