Research workbench
Cryo-EM structure of human ABCA1
Analyse Cryo-EM structure of human ABCA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XJY
- Type
- protein
- Length
- 1,901 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-binding cassette sub-family a member 1
- UniProt
- O95477
- Ligands
- NAG, BMA
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-binding cassette sub-family a member 1 | protein | 1901 | 47% helix, 4% strand | O95477 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 936 | 0.82 | 0.84 | 124 | empty |
| 2 | 991 | 0.77 | 0.80 | 108 | empty |
| 3 | 577 | 0.76 | 0.83 | 76 | empty |
| 4 | 1000 | 0.76 | 0.79 | 98 | empty |
| 5 | 554 | 0.76 | 0.83 | 86 | empty |
Modifications
Observed in the structure: 7 glycan, 4 disulfide (N-glycosylation, disulfide).
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 O95477
- Elsewhere: RCSB PDB 5XJY · PDBe 5XJY · UniProt O95477
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