1ys0

Crystal Structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the disulfide form

Method: X-RAY DIFFRACTION Dmax: 55.6 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 Fragment:catalytic domain CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.25;DTT, Tris, Ammonium Sulfate, pH 7.25, VAPOR DIFFUSION, HANGING DROP, temperature 100.0K Resolution 2.00 Å R-free 0.244

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 2–175; 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 1ys0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ys0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ys0
Deposition date deposition_date2005-02-05
Structure title titleCrystal Structure of the CDC25B phosphatase catalytic domain with the active site cysteine in the disulfide form
Keywords keywordsdisulfide bond, HYDROLASE, CELL CYCLE; HYDROLASE, CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.16
Radius of gyration Rg (electron density) rg_electron16.00
Forward intensity I(0) i07349010.00
Molecular weight molecular_weight20270.0 kDa
Excluded volume excluded_volume25558 ų
Envelope volume envelope_volume29048 ų
Hydration-shell volume shell_volume15283 ų
Envelope diameter envelope_diameter55.7
Shell Rg shell_rg21.93
Envelope Rg envelope_rg16.31
Shape Rg shape_rg16.02
Total Rg total_rg17.02
Total atoms total_atoms1428
Residues n_residues171
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 dmax55.6
Rg (real space) rg_real17.07
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real7.3490e+06
I(0) uncertainty (real space) i0_real_error8.4480e+04
Rg (reciprocal space) rg_reciprocal17.09
I(0) (reciprocal space) i0_reciprocal7349000.0000
Solution quality estimate total_estimate0.8885
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2168000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ys0a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.46 — Rhodanese/Cell cycle control phosphatase
Superfamily Superfamily superfamilyc.46.1 — Rhodanese/Cell cycle control phosphatase
Family Family familyc.46.1.1 — Cell cycle control phosphatase, catalytic domain
Domain ID domain_idd1ys0a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1ys0A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology250 — Oxidized Rhodanese; domain 1
Homologous superfamily homologous superfamily10 — Rhodanese-like domain

8. Citations (1)

9. Files and Curves (10)