Research workbench
Structure of apo-closed ABCG2
Analyse Structure of apo-closed ABCG2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VXF
- Type
- protein
- Length
- 1,130 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- EC
- 7.6.2.2
- UniProt
- Q9UNQ0
- Pockets
- 16 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 52% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Broad substrate specificity ATP-binding cassette transporter ABCG2 (EC 7.6.2.2) | protein | 565 | 52% helix, 7% strand | Q9UNQ0 |
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 956 | 0.78 | 0.80 | 98 | empty |
| 2 | 343 | 0.71 | 0.83 | 52 | empty |
| 3 | 397 | 0.68 | 0.81 | 35 | empty |
| 4 | 366 | 0.66 | 0.80 | 34 | empty |
| 5 | 90 | 0.63 | 0.89 | 22 | empty |
Interfaces
1 interface between chains.
- B–A · 3012 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (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 Q9UNQ0
- Elsewhere: RCSB PDB 6VXF · PDBe 6VXF · UniProt Q9UNQ0
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