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Crystal structure of ATP-bound human ABCF1
Analyse Crystal structure of ATP-bound human ABCF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZXD
- Type
- protein
- Length
- 955 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family F member 1
- UniProt
- Q8NE71
- Ligands
- ATP
- Pockets
- 12 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family F member 1 | protein | 464 | 40% helix, 23% strand | Q8NE71 |
| B | ATP-binding cassette sub-family F member 1 | protein | 491 | 43% helix, 21% strand | Q8NE71 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 996 | 0.76 | 0.78 | 98 | ATP |
| 2 | 522 | 0.70 | 0.79 | 58 | ATP |
| 3 | 563 | 0.67 | 0.78 | 52 | empty |
| 4 | 77 | 0.51 | 0.84 | 14 | empty |
| 5 | 172 | 0.47 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 775 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
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 Q8NE71
- Elsewhere: RCSB PDB 5ZXD · PDBe 5ZXD · UniProt Q8NE71
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