Research workbench
Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain
Analyse Structures of P-glycoprotein reveal its conformational flexibility and an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KSC
- Type
- protein
- Length
- 1,182 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug resistance protein 1A
- EC
- 3.6.3.44
- UniProt
- P21447
- Pockets
- 19 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug resistance protein 1A (EC 3.6.3.44) | protein | 1182 | 61% helix, 8% strand | P21447 |
Pockets
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.81 | 0.84 | 76 | empty |
| 2 | 629 | 0.71 | 0.78 | 55 | empty |
| 3 | 316 | 0.70 | 0.83 | 43 | empty |
| 4 | 320 | 0.69 | 0.83 | 43 | empty |
| 5 | 211 | 0.63 | 0.83 | 36 | empty |
Compared structures
- 4KSC · Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the… · 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 4KSC · PDBe 4KSC · UniProt P21447
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