Research workbench
Crystal structure of catalytically active form of human DUSP26
Analyse Crystal structure of catalytically active form of human DUSP26 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GTJ
- Type
- protein
- Length
- 668 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase 26
- EC
- 3.1.3.16, 3.1.3.48
- UniProt
- Q9BV47
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48) | protein | 166 | 48% helix, 13% strand | Q9BV47 |
| B | Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48) | protein | 168 | 46% helix, 13% strand | Q9BV47 |
| D | Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48) | protein | 168 | 46% helix, 13% strand | Q9BV47 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1166 | 0.75 | 0.78 | 118 | PO4 |
| 2 | 97 | 0.37 | 0.75 | 18 | empty |
| 3 | 101 | 0.36 | 0.74 | 17 | empty |
| 4 | 61 | 0.27 | 0.73 | 12 | empty |
| 5 | 55 | 0.27 | 0.73 | 11 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1628 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1616 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 456 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 124 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 81 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5GTJ · Crystal structure of catalytically active form of human DUSP26 · the same entry in another collection · chain D against D, TM-score 1.00
- Q9BV47 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 26 (Q9BV47) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q9BV47
- Elsewhere: RCSB PDB 5GTJ · PDBe 5GTJ · UniProt Q9BV47
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