4c9e

Mouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form II

Method: X-RAY DIFFRACTION Dmax: 106.1 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 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 (Q5M7L6) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.334
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 53–205 Chain G; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-2 × 2 (Q5M7L6) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.334

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 16 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 Author chain E; PDBConstruct 4–156; UniProt 53–205 Author chain G; PDBConstruct 4–156; UniProt 53–205

R-SPONDIN-2

XENOPUS (SILURANA) TROPICALIS

UniProt Q5M7L6

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 35–144 Chain D; UniProt 35–144 Fragment:FU1-FU2, RESIDUES 35-144 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 2 (Q5SSZ7) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.334
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 35–144 Chain H; UniProt 35–144 Fragment:FU1-FU2, RESIDUES 35-144 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 2 (Q5SSZ7) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.334

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.

6 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSPO2_XENTR
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–113; UniProt 35–144 Author chain D; PDBConstruct 4–113; UniProt 35–144 Author chain F; PDBConstruct 4–113; UniProt 35–144 Author chain H; PDBConstruct 4–113; UniProt 35–144

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 4c9e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c9e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c9e
Deposition date deposition_date2013-10-02
Structure title titleMouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form II
Keywords keywordsLIGASE-SIGNALING PROTEIN COMPLEX, WNT, RNF43, LGR4, LGR5, LGR6, RSPO, 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_guinier33.19
Radius of gyration Rg (electron density) rg_electron32.19
Forward intensity I(0) i0209519000.00
Molecular weight molecular_weight109810.0 kDa
Excluded volume excluded_volume135250 ų
Envelope volume envelope_volume188280 ų
Hydration-shell volume shell_volume47244 ų
Envelope diameter envelope_diameter113.1
Shell Rg shell_rg40.16
Envelope Rg envelope_rg31.86
Shape Rg shape_rg32.17
Total Rg total_rg32.91
Total atoms total_atoms7644
Residues n_residues1020
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 dmax106.1
Rg (real space) rg_real32.90
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real2.0950e+08
I(0) uncertainty (real space) i0_real_error2.6670e+06
Rg (reciprocal space) rg_reciprocal33.02
I(0) (reciprocal space) i0_reciprocal209500000.0000
Solution quality estimate total_estimate0.8803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.4
Skewness Skewness skewness0.040
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25390000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4c9eb_
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_idd4c9ed_
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_idd4c9ef_
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_idd4c9eh_
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 (8 domains)

Domain ID domain_id4c9eA00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9eB00
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_id4c9eC00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9eD00
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_id4c9eE00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9eF00
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_id4c9eG00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9eH00
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)