4c99

Mouse ZNRF3 ectodomain in complex with mouse RSPO2 Fu1-Fu2 crystal form I

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 53–205 Chain C; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-2 × 2 (Q8BFU0) CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.323

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 Author chain C; PDBConstruct 4–156; UniProt 53–205

R-SPONDIN-2

MUS MUSCULUS

UniProt Q8BFU0

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 37–144 Chain D; UniProt 37–144 Fragment:FU1-FU2, RESIDUES 37-144 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 2 (Q5SSZ7) CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.80 Å R-free 0.323

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSPO2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–111; UniProt 37–144 Author chain D; PDBConstruct 4–111; UniProt 37–144

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 4c99

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c99
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c99
Deposition date deposition_date2013-10-02
Structure title titleMouse ZNRF3 ectodomain in complex with mouse RSPO2 Fu1-Fu2 crystal form I
Keywords keywords;LIGASE-SIGNALING PROTEIN COMPLEX, WNT, RNF43, LGR4, LGR5, LGR6, RSPO, R-SPONDIN, R-SPO, RSPO1, RSPO3, RSPO4, RECEPTOR, MEMBRANE, SIGNALLING ;; LIGASE/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.12
Radius of gyration Rg (electron density) rg_electron27.19
Forward intensity I(0) i059609200.00
Molecular weight molecular_weight56929.0 kDa
Excluded volume excluded_volume69903 ų
Envelope volume envelope_volume94829 ų
Hydration-shell volume shell_volume29181 ų
Envelope diameter envelope_diameter89.2
Shell Rg shell_rg34.47
Envelope Rg envelope_rg27.10
Shape Rg shape_rg27.16
Total Rg total_rg28.03
Total atoms total_atoms3968
Residues n_residues514
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 dmax85.0
Rg (real space) rg_real28.02
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real5.9610e+07
I(0) uncertainty (real space) i0_real_error8.2210e+05
Rg (reciprocal space) rg_reciprocal28.06
I(0) (reciprocal space) i0_reciprocal59610000.0000
Solution quality estimate total_estimate0.9135
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.5
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.750
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7415000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4c99b_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.9 — Growth factor receptor domain
Family Family familyg.3.9.0 — automated matches
Domain ID domain_idd4c99d_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.9 — Growth factor receptor domain
Family Family familyg.3.9.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id4c99A00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c99B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology220 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Homologous superfamily homologous superfamily10 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2
Domain ID domain_id4c99C00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c99D00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology220 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Homologous superfamily homologous superfamily10 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2

8. Citations (1)

9. Files and Curves (10)