4uz6

STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM V - SOS COMPLEX - 1.9A

Method: X-RAY DIFFRACTION Dmax: 108.5 Å Quality: REASONABLE

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 81–451 Fragment:RESIDUES 81-451 Mutation:YES 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;20 %W/V PEG3350, 0.2 M AMMONIUM SULFATE 20MM SOS, pH 7.5 Resolution 1.90 Å R-free 0.235
2 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 81–451 Fragment:RESIDUES 81-451 Mutation:YES 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;20 %W/V PEG3350, 0.2 M AMMONIUM SULFATE 20MM SOS, pH 7.5 Resolution 1.90 Å R-free 0.235

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 4uz6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4uz6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4uz6
Deposition date deposition_date2014-09-04
Structure title titleSTRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM V - SOS COMPLEX - 1.9A
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_guinier32.02
Radius of gyration Rg (electron density) rg_electron31.55
Forward intensity I(0) i0118935000.00
Molecular weight molecular_weight82852.0 kDa
Excluded volume excluded_volume101850 ų
Envelope volume envelope_volume125070 ų
Hydration-shell volume shell_volume34270 ų
Envelope diameter envelope_diameter109.5
Shell Rg shell_rg37.08
Envelope Rg envelope_rg31.66
Shape Rg shape_rg31.51
Total Rg total_rg32.10
Total atoms total_atoms5802
Residues n_residues706
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 dmax108.5
Rg (real space) rg_real32.29
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.1890e+08
I(0) uncertainty (real space) i0_real_error1.8650e+06
Rg (reciprocal space) rg_reciprocal32.18
I(0) (reciprocal space) i0_reciprocal118900000.0000
Solution quality estimate total_estimate0.6679
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.0
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18020000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.865; Smooth: 0.873

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_idd4uz6a_
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_idd4uz6b_
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)