Research workbench
Crystal structure of the Catalytic Domain of Human DUSP12
Analyse Crystal structure of the Catalytic Domain of Human DUSP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JNB
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3
- Source
- Homo sapiens
- Molecule
- Dual specificity protein phosphatase 12
- EC
- 3.1.3.16, 3.1.3.48
- UniProt
- Q9UNI6
- Ligands
- SO4
Structure
x-ray diffraction · resolution 3 · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase 12 (EC 3.1.3.16, 3.1.3.48) | protein | 160 | 41% helix, 18% strand | Q9UNI6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4JNB · Crystal structure of the catalytic domain of human DUSP12 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNI6 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 12 (Q9UNI6) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9UNI6
- Elsewhere: RCSB PDB 4JNB · PDBe 4JNB · UniProt Q9UNI6
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