2a2k

Crystal Structure of an active site mutant, C473S, of Cdc25B Phosphatase Catalytic Domain

Method: X-RAY DIFFRACTION Dmax: 55.4 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 377–550 Fragment:Catalytic Domain Mutation:C473S CL CHLORIDE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;DTT, Ammonium Sulfate, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.52 Å R-free 0.191

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 377–550

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 2a2k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2a2k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2a2k
Deposition date deposition_date2005-06-22
Structure title titleCrystal Structure of an active site mutant, C473S, of Cdc25B Phosphatase Catalytic Domain
Keywords keywordsPHOSPHATASE, DUAL SPECIFICITY, SUBSTRATE TRAPPING, ACTIVE SITE MUTANT, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.05
Radius of gyration Rg (electron density) rg_electron15.95
Forward intensity I(0) i07485040.00
Molecular weight molecular_weight20385.0 kDa
Excluded volume excluded_volume25626 ų
Envelope volume envelope_volume28675 ų
Hydration-shell volume shell_volume15127 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg21.93
Envelope Rg envelope_rg16.31
Shape Rg shape_rg15.97
Total Rg total_rg16.96
Total atoms total_atoms1434
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 dmax55.4
Rg (real space) rg_real16.97
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real7.4850e+06
I(0) uncertainty (real space) i0_real_error9.2860e+04
Rg (reciprocal space) rg_reciprocal16.98
I(0) (reciprocal space) i0_reciprocal7485000.0000
Solution quality estimate total_estimate0.8872
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.212
Kurtosis Kurtosis kurtosis-0.327
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1965000.0000
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: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2a2ka_
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

CATH v4.4 (1 domains)

Domain ID domain_id2a2kA00
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)