4uyu

STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I IODIDE COMPLEX - 2.3A

Method: X-RAY DIFFRACTION Dmax: 95.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 81–451 Mutation:YES NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 IOD IODIDE ION × 5 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;20 %W/V PEG 3350 0.1 M BT PROPANE PH 6.5 0.2 M NAI Resolution 2.30 Å R-free 0.243
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 81–451 Mutation:YES NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 IOD IODIDE ION × 6 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;20 %W/V PEG 3350 0.1 M BT PROPANE PH 6.5 0.2 M NAI Resolution 2.30 Å R-free 0.243

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 148 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 4–374; UniProt 81–451 Author chain B; PDBConstruct 4–374; UniProt 81–451

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 4uyu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4uyu
Deposition date deposition_date2014-09-03
Structure title titleSTRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I IODIDE COMPLEX - 2.3A
Keywords keywordsHYDROLASE, 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_guinier30.71
Radius of gyration Rg (electron density) rg_electron30.01
Forward intensity I(0) i0113901000.00
Molecular weight molecular_weight80566.0 kDa
Excluded volume excluded_volume98626 ų
Envelope volume envelope_volume124120 ų
Hydration-shell volume shell_volume34220 ų
Envelope diameter envelope_diameter97.0
Shell Rg shell_rg37.61
Envelope Rg envelope_rg29.64
Shape Rg shape_rg29.99
Total Rg total_rg30.72
Total atoms total_atoms5582
Residues n_residues690
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 dmax95.2
Rg (real space) rg_real30.71
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.1390e+08
I(0) uncertainty (real space) i0_real_error1.7270e+06
Rg (reciprocal space) rg_reciprocal30.71
I(0) (reciprocal space) i0_reciprocal113900000.0000
Solution quality estimate total_estimate0.9048
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.258
Kurtosis Kurtosis kurtosis-0.706
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14610000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4uyua_
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
Domain ID domain_idd4uyub_
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)