9t0a

X-ray structure of the complex between the catalytic domain of CDC25B C473S and 3-O-methylfluorescein phosphate (3-OMFP)

Method: X-RAY DIFFRACTION Dmax: 58.1 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

M-phase inducer phosphatase 2

Homo sapiens

UniProt P30305

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 391–564 Mutation:C473S A1JSQ [(1~{R})-6'-methoxy-3-oxidanylidene-spiro[2-benzofuran-1,9'-xanthene]-3'-yl] dihydrogen phosphate × 1 A1JSP [(1~{S})-6'-methoxy-3-oxidanylidene-spiro[2-benzofuran-1,9'-xanthene]-3'-yl] dihydrogen phosphate × 1 CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;3.8 M NaCl, 0.1 M HEPES pH 7.5, and 1.2% v/v 2-propanol Resolution 2.04 Å R-free 0.214

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MPIP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–197; UniProt 391–564

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9t0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t0a
Deposition date deposition_date2025-10-16
Structure title titleX-ray structure of the complex between the catalytic domain of CDC25B C473S and 3-O-methylfluorescein phosphate (3-OMFP)
Keywords keywordsCDC25B, Catalytic Domain, Phosphatase, Cell Division Cycle 25B, substrate, 3-O-methylfluorescein phosphate, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.49
Radius of gyration Rg (electron density) rg_electron16.55
Forward intensity I(0) i016307100.00
Molecular weight molecular_weight20576.0 kDa
Excluded volume excluded_volume19973 ų
Envelope volume envelope_volume31363 ų
Hydration-shell volume shell_volume15932 ų
Envelope diameter envelope_diameter58.7
Shell Rg shell_rg22.54
Envelope Rg envelope_rg16.95
Shape Rg shape_rg16.53
Total Rg total_rg17.32
Total atoms total_atoms1553
Residues n_residues186
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax58.1
Rg (real space) rg_real17.42
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.6310e+07
I(0) uncertainty (real space) i0_real_error1.6760e+05
Rg (reciprocal space) rg_reciprocal17.43
I(0) (reciprocal space) i0_reciprocal16310000.0000
Solution quality estimate total_estimate0.8822
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.286
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha3816000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)