Research workbench
Crystal structure of human DUSP28(Y102H)
Analyse Crystal structure of human DUSP28(Y102H) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y16
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity phosphatase 28
- EC
- 3.1.3.16, 3.1.3.48
- UniProt
- Q4G0W2
- Ligands
- CL, PO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity phosphatase 28 (EC 3.1.3.16, 3.1.3.48) | protein | 148 | 45% helix, 16% strand | Q4G0W2 |
| B | Dual specificity phosphatase 28 (EC 3.1.3.16, 3.1.3.48) | protein | 146 | 46% helix, 14% strand | Q4G0W2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.38 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 651 Ų buried · 5 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 Q4G0W2
- Elsewhere: RCSB PDB 5Y16 · PDBe 5Y16 · UniProt Q4G0W2
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