Research workbench
Structure of ATP-free human ABCA4
Analyse Structure of ATP-free human ABCA4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LKP
- Type
- protein
- Length
- 1,941 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinal-specific phospholipid-transporting ATPase ABCA4
- EC
- 7.6.2.1
- UniProt
- P78363
- Ligands
- CLR, POV, AJP, NAG, BMA
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinal-specific phospholipid-transporting ATPase ABCA4 (EC 7.6.2.1) | protein | 1941 | 49% helix, 10% strand | P78363 |
Ligands and binding sites
- CLR · Cholesterol · ligand · 7 copies · chains A
- POV · (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate · ligand · 7 copies · chains A
- AJP · Digitonin · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 4 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.84 | 0.85 | 87 | empty |
| 2 | 916 | 0.79 | 0.81 | 93 | empty |
| 3 | 389 | 0.70 | 0.82 | 53 | empty |
| 4 | 214 | 0.69 | 0.86 | 35 | empty |
| 5 | 226 | 0.68 | 0.85 | 37 | empty |
Modifications
Observed in the structure: 9 glycan, 6 disulfide, 1 covalent (N-glycosylation, disulfide, covalent ligand, glycosylation).
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 P78363
- Elsewhere: RCSB PDB 7LKP · PDBe 7LKP · UniProt P78363
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