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Crystal structure of an active site mutant, C473S, of CDC25B phosphatase catalytic domain
Analyse Crystal structure of an active site mutant, C473S, of CDC25B phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A2K
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- M-phase inducer phosphatase 2
- EC
- 3.1.3.48
- UniProt
- P30305
- Ligands
- CL, SO4
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | M-phase inducer phosphatase 2 (EC 3.1.3.48) | protein | 171 | 33% helix, 18% strand | P30305 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.51 | 0.82 | 23 | CL, SO4 |
| 2 | 85 | 0.39 | 0.77 | 15 | empty |
Compared structures
- 2A2K · Crystal Structure of an active site mutant, C473S, of Cdc25B Phosphatase Catalytic Domain · 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 0.99
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 2A2K · PDBe 2A2K · UniProt P30305
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