Research workbench
Structure of the human mitochondrial ABC transporter, ABCB10
Analyse Structure of the human mitochondrial ABC transporter, ABCB10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AYT
- Type
- protein
- Length
- 564 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family B member 10 mitochondrial
- UniProt
- Q9NRK6
- Ligands
- CDL, GLY, ACP, MG
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family B member 10 mitochondrial | protein | 564 | 65% helix, 10% strand | Q9NRK6 |
Ligands and binding sites
- CDL · Cardiolipin · ligand · 2 copies · chains A
- GLY · Glycine · ligand · chains A
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- LMT · Dodecyl-beta-D-maltoside · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 409 | 0.59 | 0.75 | 36 | empty |
| 2 | 189 | 0.50 | 0.76 | 28 | LMT |
| 3 | 99 | 0.49 | 0.81 | 23 | empty |
| 4 | 55 | 0.30 | 0.75 | 11 | empty |
Compared structures
- 4AYT · Structure of the human mitochondrial ABC transporter, ABCB10 · 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 0.98
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 Q9NRK6
- Elsewhere: RCSB PDB 4AYT · PDBe 4AYT · UniProt Q9NRK6
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