4uza

STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VIII - PHOSPHATE COMPLEX - 2.4A

Method: X-RAY DIFFRACTION Dmax: 65.0 Å Quality: EXCELLENT

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

PROTEIN NOTUM HOMOLOG

HOMO SAPIENS

UniProt Q6P988

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 80–452 Fragment:RESIDUES 80-452 Mutation:YES NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 PO4 PHOSPHATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.3;0.630 M K2HPO4 1.170 M NAH2PO4 6.300 PH FINAL PH Resolution 2.40 Å R-free 0.271

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.

140 other PDB entries and 149 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NOTUM_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–375; UniProt 80–452

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 4uza

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4uza
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4uza
Deposition date deposition_date2014-09-04
Structure title titleSTRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM VIII - PHOSPHATE COMPLEX - 2.4A
Keywords keywordsHYDROLASE, WNT, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.28
Radius of gyration Rg (electron density) rg_electron19.87
Forward intensity I(0) i029549500.00
Molecular weight molecular_weight40632.0 kDa
Excluded volume excluded_volume50338 ų
Envelope volume envelope_volume58936 ų
Hydration-shell volume shell_volume23845 ų
Envelope diameter envelope_diameter65.0
Shell Rg shell_rg27.27
Envelope Rg envelope_rg20.26
Shape Rg shape_rg19.83
Total Rg total_rg20.88
Total atoms total_atoms2859
Residues n_residues355
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 dmax65.0
Rg (real space) rg_real21.11
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real2.9550e+07
I(0) uncertainty (real space) i0_real_error3.0470e+05
Rg (reciprocal space) rg_reciprocal21.14
I(0) (reciprocal space) i0_reciprocal29550000.0000
Solution quality estimate total_estimate0.9037
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.8
Skewness Skewness skewness0.080
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5062000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4uzaa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.42 — Pectinacetylesterase-like

8. Citations (1)

9. Files and Curves (10)