MolNFT v1 · #84215 · protein
Structure of the human mitochondrial ABC transporter, ABCB10 (nucleotide-free form)
3ZDQ · ATP-binding cassette sub-family B member 10, mitochondrial: “Structure of the human mitochondrial ABC transporter, ABCB10 (nucleotide-free form)”. X-ray diffraction, 2 ligands (CDL, GLY), 5 pockets (best druggability 0.58). MolNFT…
- PDB
- 3ZDQ
- Type
- protein
- Length
- 570 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
- EC
- 3.6.3.43
- UniProt
- Q9NRK6
- Ligands
- CDL, GLY
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family B member 10, mitochondrial (EC 3.6.3.43) | protein | 570 | 66% helix, 10% strand | Q9NRK6 |
Ligands and binding sites
- CDL · Cardiolipin · ligand · 2 copies · chains A
- GLY · Glycine · ligand · 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
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.58 | 0.75 | 41 | empty |
| 2 | 101 | 0.48 | 0.81 | 21 | empty |
| 3 | 169 | 0.48 | 0.76 | 23 | LMT |
| 4 | 52 | 0.29 | 0.75 | 10 | empty |
| 5 | 55 | 0.29 | 0.74 | 19 | empty |
Compared structures
- 3ZDQ · Structure of the human mitochondrial ABC transporter, ABCB10 (nucleotide-free 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 0.98
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 3ZDQ · PDBe 3ZDQ · UniProt Q9NRK6
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