4c9a

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

Method: X-RAY DIFFRACTION Dmax: 86.9 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 1–165 Chain C; UniProt 1–165 Fragment:ECTODOMAIN, RESIDUES 1-165 R-SPONDIN-2 × 2 (Q5M7L6) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å R-free 0.273

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 1–165; UniProt 1–165 Author chain C; PDBConstruct 1–165; UniProt 1–165

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 32–152 Chain D; UniProt 35–144 Fragment:FU1-FU2, RESIDUES 32-152 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 2.40 Å R-free 0.273

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 16 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 1–121; UniProt 32–152 Author chain D; 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 4c9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c9a
Deposition date deposition_date2013-10-02
Structure title titleMouse ZNRF3 ectodomain in complex with Xenopus RSPO2 Fu1-Fu2 (Seleno Met) crystal form I
Keywords keywordsLIGASE, WNT, LGR4, LGR5, LGR6, RSPO, R-SPONDIN, R-SPO, RSPO1, RSPO2, RSPO3, RSPO4, RECEPTOR, SIGNALLING; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.89
Radius of gyration Rg (electron density) rg_electron27.07
Forward intensity I(0) i055304300.00
Molecular weight molecular_weight54922.0 kDa
Excluded volume excluded_volume67489 ų
Envelope volume envelope_volume91542 ų
Hydration-shell volume shell_volume28503 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg34.06
Envelope Rg envelope_rg27.14
Shape Rg shape_rg27.04
Total Rg total_rg27.88
Total atoms total_atoms3815
Residues n_residues505
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 dmax86.9
Rg (real space) rg_real27.82
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real5.5300e+07
I(0) uncertainty (real space) i0_real_error8.1880e+05
Rg (reciprocal space) rg_reciprocal27.84
I(0) (reciprocal space) i0_reciprocal55310000.0000
Solution quality estimate total_estimate0.9103
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.741
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6717000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4c9ab_
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_idd4c9ad_
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_id4c9aA00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9aB00
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_id4c9aC00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4c9aD00
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)