Research workbench
Structure of the human mitochondrial ABC transporter, ABCB10 (plate form)
Analyse Structure of the human mitochondrial ABC transporter, ABCB10 (plate form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AYW
- Type
- protein
- Length
- 560 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- HOMO SAPIENS
- Molecule
- ATP-binding cassette sub-family B member 10
- UniProt
- Q9NRK6
- Ligands
- ANP, Y01
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · resolution 3.3 · 1 distinct chain · 64% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family B member 10 | protein | 560 | 64% helix, 11% strand | Q9NRK6 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- Y01 · Cholesterol hemisuccinate · ligand · chains A
- LMT · Dodecyl-beta-D-maltoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.79 | 0.97 | 28 | empty |
| 2 | 293 | 0.53 | 0.75 | 26 | empty |
| 3 | 219 | 0.51 | 0.75 | 26 | empty |
| 4 | 102 | 0.44 | 0.79 | 17 | empty |
| 5 | 93 | 0.40 | 0.77 | 20 | empty |
Compared structures
- 4AYW · Structure of the human mitochondrial ABC transporter, ABCB10 (plate form) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NRK6 · AlphaFold monomer V2.0 prediction for ATP-binding cassette sub-family B member 10… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q9NRK6
- Elsewhere: RCSB PDB 4AYW · PDBe 4AYW · UniProt Q9NRK6
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