Research workbench
Crystal structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the disulfide form
Analyse Crystal structure of the CDC25B phosphatase catalytic domain with the active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YS0
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P30305
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 171 | — | P30305 |
Compared structures
- 1YS0 · Crystal Structure of the CDC25B phosphatase catalytic domain with the active site… · the same entry in another collection · chain A against A, TM-score 1.00
- P30305 · AlphaFold monomer V2.0 prediction for M-phase inducer phosphatase 2 (P30305) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P30305
- Elsewhere: RCSB PDB 1YS0 · PDBe 1YS0 · UniProt P30305
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