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Structure of human dual-specificity phosphatase 27
Analyse Structure of human dual-specificity phosphatase 27 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Y96
- Type
- protein
- Length
- 340 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity phosphatase DUPD1
- EC
- 3.1.3.16, 3.1.3.48
- UniProt
- Q68J44
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity phosphatase DUPD1 (EC 3.1.3.16, 3.1.3.48) | protein | 175 | 47% helix, 13% strand | Q68J44 |
| B | Dual specificity phosphatase DUPD1 (EC 3.1.3.16, 3.1.3.48) | protein | 165 | 48% helix, 13% strand | Q68J44 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.50 | 0.75 | 32 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1551 Ų buried · 13 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 Q68J44
- Elsewhere: RCSB PDB 2Y96 · PDBe 2Y96 · UniProt Q68J44
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