MolNFT v1 · #3582 · protein
Human CDC25B catalytic domain with tungstate
1CWS · CDC25 B-type tyrosine phosphatase: “Human CDC25B catalytic domain with tungstate”. X-ray diffraction, 3 ligands (WO4, SO4, CL), 3 pockets (best druggability 0.46). MolNFT v1 #3582 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1CWS
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CDC25 B-type tyrosine phosphatase
- UniProt
- P30305
- Ligands
- WO4, SO4, CL
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CDC25 B-type tyrosine phosphatase | protein | 178 | 32% helix, 17% strand | P30305 |
Ligands and binding sites
- WO4 · Tungstate(vi)ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- CL · Chloride ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.46 | 0.79 | 17 | BME |
| 2 | 53 | 0.38 | 0.81 | 15 | CL |
| 3 | 62 | 0.32 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 P30305
- Elsewhere: RCSB PDB 1CWS · PDBe 1CWS · UniProt P30305
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