4c8p

mouse ZNRF3 ectodomain crystal form V, disulfide-bridged S90C variant

Method: X-RAY DIFFRACTION Dmax: 57.5 Å Quality: GOOD

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

E3 UBIQUITIN-PROTEIN LIGASE ZNRF3

MUS MUSCULUS

UniProt Q5SSZ7

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 Mutation:YES No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.10 Å R-free 0.286

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.

10 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZNRF3_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–156; UniProt 53–205

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 4c8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c8p
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4c8p
Deposition date deposition_date2013-10-01
Structure title titlemouse ZNRF3 ectodomain crystal form V, disulfide-bridged S90C variant
Keywords keywordsLIGASE, WNT, RNF43, LGR4, LGR5, LGR6, RSPO, R-SPONDIN, R-SPO, RSPO1, RSPO2, RSPO3, RSPO4, RECEPTOR, MEMBRANE, SIGNALLING; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.50
Radius of gyration Rg (electron density) rg_electron15.17
Forward intensity I(0) i04805420.00
Molecular weight molecular_weight15706.0 kDa
Excluded volume excluded_volume19745 ų
Envelope volume envelope_volume23007 ų
Hydration-shell volume shell_volume13211 ų
Envelope diameter envelope_diameter59.4
Shell Rg shell_rg20.65
Envelope Rg envelope_rg15.64
Shape Rg shape_rg15.18
Total Rg total_rg16.25
Total atoms total_atoms1103
Residues n_residues144
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 dmax57.5
Rg (real space) rg_real16.49
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.8050e+06
I(0) uncertainty (real space) i0_real_error6.5020e+04
Rg (reciprocal space) rg_reciprocal16.49
I(0) (reciprocal space) i0_reciprocal4805000.0000
Solution quality estimate total_estimate0.7572
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.427
Kurtosis Kurtosis kurtosis0.207
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1210000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.616; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4c8pA00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)