Research workbench
Crystal structure of catalytic domain of dual specificity phosphatase 26, MS0830 from homo sapiens
Analyse Crystal structure of catalytic domain of dual specificity phosphatase 26… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E0T
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity phosphatase 26
- EC
- 3.1.3.48
- UniProt
- Q9BV47
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity phosphatase 26 (EC 3.1.3.48) | protein | 150 | 47% helix, 14% strand | Q9BV47 |
Compared structures
- 2E0T · Crystal structure of catalytic domain of dual specificity phosphatase 26, MS0830 from… · the same entry in another collection · chain A against A, 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 0.82
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 2E0T · PDBe 2E0T · UniProt Q9BV47
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