Research workbench
Crystal structure of ciona intestinalis voltage sensor-containing phosphatase (ci-vsp), residues 241-576(C363S), complexed with D-myo- inositol-1,4,5-triphosphate
Analyse Crystal structure of ciona intestinalis voltage sensor-containing phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V0H
- Type
- protein
- Length
- 653 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-sensor containing phosphatase
- UniProt
- Q4W8A1
- Ligands
- I3P
- Pockets
- 9 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-sensor containing phosphatase | protein | 326 | 26% helix, 30% strand | Q4W8A1 |
| B | Voltage-sensor containing phosphatase | protein | 327 | 26% helix, 32% strand | Q4W8A1 |
Ligands and binding sites
- I3P · D-myo-inositol-1,4,5-triphosphate · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.45 | 0.76 | 32 | empty |
| 2 | 120 | 0.45 | 0.78 | 24 | empty |
| 3 | 135 | 0.45 | 0.77 | 26 | I3P |
| 4 | 115 | 0.43 | 0.77 | 27 | empty |
| 5 | 110 | 0.43 | 0.77 | 18 | I3P |
Interfaces
1 interface between chains.
- A–B · 350 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3V0H · Crystal structure of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP)… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q4W8A1
- Elsewhere: RCSB PDB 3V0H · PDBe 3V0H · UniProt Q4W8A1
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