MolNFT v1 · #151045 · protein
Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and magnesium
6HBU · ATP-binding cassette sub-family G member 2: “Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and magnesium”. Electron microscopy, 2 ligands (ATP, MG), 20 pockets (best druggability 0.78). MolNFT v1 #151045 on GenesisL1: 3D…
- PDB
- 6HBU
- Type
- protein
- Length
- 1,168 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family G member 2
- UniProt
- Q9UNQ0
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP-binding cassette sub-family G member 2 | protein | 584 | 51% helix, 9% strand | Q9UNQ0 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 262 | 0.78 | 0.90 | 30 | empty |
| 2 | 290 | 0.78 | 0.90 | 50 | ATP |
| 3 | 241 | 0.77 | 0.91 | 33 | empty |
| 4 | 263 | 0.77 | 0.90 | 44 | ATP |
| 5 | 109 | 0.68 | 0.91 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 4526 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6HBU · Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNQ0 · AlphaFold monomer V2.0 prediction for broad substrate specificity ATP-binding cassette… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 6HBU · PDBe 6HBU · UniProt Q9UNQ0
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