GL1X · GenesisL1 explorer

Research workbench

Human CDC25B catalytic domain without ion in catalytic site

Analyse Human CDC25B catalytic domain without ion in catalytic site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CWR
Type
protein
Length
177 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (M-phase inducer phosphatase 2 (CDC25B))
EC
3.1.3.48
UniProt
P30305
Ligands
SO4
Pockets
3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (M-phase inducer phosphatase 2 (CDC25B)) (EC 3.1.3.48)protein17732% helix, 17% strandP30305

Ligands and binding sites

  • SO4 · Sulfate 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.480.7917BME
2830.420.7922empty
3670.350.7717empty

Modifications

Observed in the structure: 1 covalent, 1 disulfide (additive adduct, disulfide).

Compared structures

  • 1CWR · Human CDC25B catalytic domain without ion in catalytic 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 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.