4uyz

STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II - 2.8A

Method: X-RAY DIFFRACTION Dmax: 114.7 Å Quality: GOOD

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 38–496 Fragment:RESIDUES 38-496 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.293
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 38–496 Fragment:RESIDUES 38-496 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.293
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 38–496 Fragment:RESIDUES 38-496 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.293
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 38–496 Fragment:RESIDUES 38-496 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.80 Å R-free 0.293

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 146 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 4–462; UniProt 38–496 Author chain B; PDBConstruct 4–462; UniProt 38–496 Author chain C; PDBConstruct 4–462; UniProt 38–496 Author chain D; PDBConstruct 4–462; UniProt 38–496

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 4uyz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4uyz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4uyz
Deposition date deposition_date2014-09-03
Structure title titleSTRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II - 2.8A
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_guinier40.56
Radius of gyration Rg (electron density) rg_electron39.71
Forward intensity I(0) i0379373000.00
Molecular weight molecular_weight156180.0 kDa
Excluded volume excluded_volume194030 ų
Envelope volume envelope_volume267380 ų
Hydration-shell volume shell_volume55472 ų
Envelope diameter envelope_diameter123.4
Shell Rg shell_rg46.47
Envelope Rg envelope_rg38.49
Shape Rg shape_rg39.69
Total Rg total_rg40.16
Total atoms total_atoms10991
Residues n_residues1396
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 dmax114.7
Rg (real space) rg_real40.34
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real3.7940e+08
I(0) uncertainty (real space) i0_real_error6.8300e+06
Rg (reciprocal space) rg_reciprocal40.56
I(0) (reciprocal space) i0_reciprocal379500000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.8
Skewness Skewness skewness-0.083
Kurtosis Kurtosis kurtosis-0.825
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89690000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.417

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4uyza_
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_idd4uyzb_
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_idd4uyzc_
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)