Research workbench
Cryo-EM structure of ATP-bound ABCA3
Analyse Cryo-EM structure of ATP-bound ABCA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W02
- Type
- protein
- Length
- 1,566 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipid-transporting ATPase ABCA3
- EC
- 7.6.2.1, 7.6.2.2
- UniProt
- Q99758
- Ligands
- ATP, NAG, MG
- Pockets
- 18 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 44% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipid-transporting ATPase ABCA3 (EC 7.6.2.1, 7.6.2.2) | protein | 1566 | 44% helix, 12% strand | Q99758 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.83 | 0.85 | 95 | empty |
| 2 | 1162 | 0.82 | 0.83 | 134 | ATP, MG |
| 3 | 1126 | 0.82 | 0.83 | 118 | empty |
| 4 | 421 | 0.72 | 0.82 | 31 | empty |
| 5 | 63 | 0.68 | 0.95 | 23 | empty |
Modifications
Observed in the structure: 2 glycan, 1 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 Q99758
- Elsewhere: RCSB PDB 7W02 · PDBe 7W02 · UniProt Q99758
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