Research workbench
Crystal structure of arabidopsis thaliana plant and fungi atypical dual specificity phosphatase 1(ATPFA-DSP1 ) CYS150SER in complex with phosphate in conformation a (PI(A))
Analyse Crystal structure of arabidopsis thaliana plant and fungi atypical dual… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MOD
- Type
- protein
- Length
- 325 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase DSP1
- EC
- 3.1.3.48
- UniProt
- Q9ZVN4
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase DSP1 (EC 3.1.3.48) | protein | 164 | 44% helix, 13% strand | Q9ZVN4 |
| B | Tyrosine-protein phosphatase DSP1 (EC 3.1.3.48) | protein | 161 | 44% helix, 14% strand | Q9ZVN4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.55 | 0.82 | 21 | empty |
| 2 | 53 | 0.54 | 0.89 | 20 | PO4 |
| 3 | 57 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1175 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7MOD · Crystal Structure of Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ZVN4 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase DSP1 (Q9ZVN4) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9ZVN4
- Elsewhere: RCSB PDB 7MOD · PDBe 7MOD · UniProt Q9ZVN4
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