Research workbench
The structure of human ABCG5/ABCG8 purified from yeast
Analyse The structure of human ABCG5/ABCG8 purified from yeast in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R89
- Type
- protein
- Length
- 1,332 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Homo sapiens; Mus musculus
- Molecule
- ATP-binding cassette sub-family G member 5; ATP-binding cassette sub-family G member 8…
- EC
- 7.6.2.-
- UniProt
- Q9H222, Q9H221
- Ligands
- ERG
- Pockets
- 14 · best druggability 0.79
Structure
electron microscopy · resolution 2.6 · 4 distinct chains · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family G member 5 (EC 7.6.2.-) | protein | 584 | 58% helix, 11% strand | Q9H222 |
| B | ATP-binding cassette sub-family G member 8 (EC 7.6.2.-) | protein | 529 | 53% helix, 12% strand | Q9H221 |
| C | 2C7 Fab heavy chain | protein | 114 | 5% helix, 39% strand | — |
| D | 2C7 Fab light chain | protein | 105 | 3% helix, 50% strand | — |
Ligands and binding sites
- ERG · Ergosterol · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.79 | 0.82 | 89 | ERG |
| 2 | 525 | 0.75 | 0.83 | 52 | empty |
| 3 | 84 | 0.75 | 0.97 | 22 | empty |
| 4 | 285 | 0.72 | 0.85 | 41 | empty |
| 5 | 59 | 0.69 | 0.97 | 21 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2671 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 780 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 460 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 382 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 45 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7R89 · The structure of human ABCG5/ABCG8 purified from yeast · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H222 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family G member 5 (Q9H222) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9H221 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family G member 8 (Q9H221) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q9H222
- Every structure of UniProt Q9H221
- Elsewhere: RCSB PDB 7R89 · PDBe 7R89 · UniProt Q9H222 · UniProt Q9H221
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