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Crystal structure of an active site mutant, C473D, of CDC25B phosphatase catalytic domain

Analyse Crystal structure of an active site mutant, C473D, 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: 2IFV
Type: protein
Length: 175 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
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	M-phase inducer phosphatase 2 (EC 3.1.3.48)	protein	175	33% helix, 17% strand	P30305

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.51	0.80	23	CL
2	97	0.44	0.79	17	empty
3	67	0.36	0.78	18	empty

Compared structures

2IFV · Crystal structure of an active site mutant, C473D, 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 2IFV · PDBe 2IFV · UniProt P30305

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