Research workbench
Crystal structure of DUSP22 MUTANT_C88S
Analyse Crystal structure of DUSP22 MUTANT_C88S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L1S
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein phosphatase 22
- EC
- 3.1.3.16, 3.1.3.48
- UniProt
- Q9NRW4
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein phosphatase 22 (EC 3.1.3.16, 3.1.3.48) | protein | 157 | 47% helix, 17% strand | Q9NRW4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q9NRW4
- Elsewhere: RCSB PDB 6L1S · PDBe 6L1S · UniProt Q9NRW4
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