Research workbench
Molecular structure of human P-glycoprotein in the ATP-bound, outward- facing conformation
Analyse Molecular structure of human P-glycoprotein in the ATP-bound, outward- facing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C0V
- Type
- protein
- Length
- 1,154 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug resistance protein 1
- EC
- 3.6.3.44
- UniProt
- P08183
- Ligands
- ATP, MG
- Pockets
- 15 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug resistance protein 1 (EC 3.6.3.44) | protein | 1154 | 62% helix, 9% strand | P08183 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1144 | 0.88 | 0.89 | 98 | empty |
| 2 | 666 | 0.86 | 0.91 | 83 | ATP, MG |
| 3 | 539 | 0.85 | 0.91 | 66 | ATP, MG |
| 4 | 1085 | 0.84 | 0.84 | 109 | empty |
| 5 | 508 | 0.74 | 0.83 | 72 | empty |
Compared structures
- 6C0V · Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation · the same entry in another collection · chain A against A, TM-score 1.00
- P08183 · AlphaFold monomer V2.0 prediction for ATP-dependent translocase ABCB1 (P08183) · a predicted model of the same protein · chain A against A, TM-score 0.70
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 P08183
- Elsewhere: RCSB PDB 6C0V · PDBe 6C0V · UniProt P08183
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