1cwt

HUMAN CDC25B CATALYTIC DOMAIN WITH METHYL MERCURY

Method: X-RAY DIFFRACTION Dmax: 58.7 Å Quality: GOOD

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

CDC25 B-TYPE TYROSINE PHOSPHATASE

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 347–524 Fragment:CATALYTIC DOMAIN SO4 SULFATE ION × 2 CL CHLORIDE ION × 1 MMC METHYL MERCURY ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 9;4 MICROLITERS PROTEIN (10 MG/ ML IN 50 MM TRISHCL, CH(3)HGCL,1% BME AT PH 9.0) MIXED WITH 4 MICROLITERS WELL BUFFER (1.8 (NH4)2SO4, 0.5 M NACL, 0.1 M TRISHCL, 0.25 BME) AT 4 DEG. C Resolution 2.30 Å

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 1–178; UniProt 347–524

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 1cwt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cwt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cwt
Deposition date deposition_date1999-08-26
Structure title titleHUMAN CDC25B CATALYTIC DOMAIN WITH METHYL MERCURY
Keywords keywordsHYDROLASE, CELL CYCLE PHOSPHATASE, DUAL SPECIFICITY PROTEIN PHOSPHATASE, CDC25, CDC25B, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.51
Radius of gyration Rg (electron density) rg_electron16.43
Forward intensity I(0) i08721210.00
Molecular weight molecular_weight21370.0 kDa
Excluded volume excluded_volume26521 ų
Envelope volume envelope_volume30611 ų
Hydration-shell volume shell_volume15699 ų
Envelope diameter envelope_diameter58.0
Shell Rg shell_rg22.44
Envelope Rg envelope_rg16.81
Shape Rg shape_rg16.49
Total Rg total_rg17.29
Total atoms total_atoms1489
Residues n_residues178
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 dmax58.7
Rg (real space) rg_real17.43
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real8.7210e+06
I(0) uncertainty (real space) i0_real_error1.0130e+05
Rg (reciprocal space) rg_reciprocal17.44
I(0) (reciprocal space) i0_reciprocal8721000.0000
Solution quality estimate total_estimate0.8724
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.275
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1805000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cwta_
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_id1cwtA00
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)