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Crystal structure of the bar-pH domain of ACAP1
Analyse Crystal structure of the bar-pH domain of ACAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NSW
- Type
- protein
- Length
- 730 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arf-gap with coiled-coil, ank repeat and pH domain- containing protein 1
- UniProt
- Q15027
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arf-gap with coiled-coil, ank repeat and pH domain- containing protein 1 | protein | 368 | 67% helix, 13% strand | Q15027 |
| B | Arf-gap with coiled-coil, ank repeat and pH domain- containing protein 1 | protein | 362 | 67% helix, 13% strand | Q15027 |
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.82 | 0.98 | 35 | empty |
| 2 | 179 | 0.53 | 0.79 | 24 | empty |
| 3 | 155 | 0.48 | 0.77 | 21 | empty |
| 4 | 102 | 0.48 | 0.80 | 23 | empty |
| 5 | 101 | 0.45 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 6142 Ų buried · 46 hydrogen bonds · protein-protein
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 Q15027
- Elsewhere: RCSB PDB 4NSW · PDBe 4NSW · UniProt Q15027
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