Research workbench
Crystal structure of pten-like domain of ci-vsp (236-576)
Analyse Crystal structure of pten-like domain of ci-vsp (236-576) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AWF
- Type
- protein
- Length
- 922 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-sensor containing phosphatase
- EC
- 3.1.3.-
- UniProt
- Q4W8A1
- Ligands
- SO4
- Pockets
- 10 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Voltage-sensor containing phosphatase (EC 3.1.3.-) | protein | 304 | 29% helix, 31% strand | Q4W8A1 |
| B | Voltage-sensor containing phosphatase (EC 3.1.3.-) | protein | 308 | 28% helix, 33% strand | Q4W8A1 |
| C | Voltage-sensor containing phosphatase (EC 3.1.3.-) | protein | 310 | 28% helix, 31% strand | Q4W8A1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.70 | 0.79 | 56 | SO4 |
| 2 | 211 | 0.54 | 0.78 | 39 | empty |
| 3 | 141 | 0.48 | 0.78 | 25 | empty |
| 4 | 134 | 0.47 | 0.78 | 22 | empty |
| 5 | 141 | 0.44 | 0.76 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–C · 403 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 386 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 107 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3AWF · Crystal structure of Pten-like domain of Ci-VSP (236-576) · 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 3AWF · PDBe 3AWF · UniProt Q4W8A1
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