4cdk

Structure of ZNRF3-RSPO1

Method: X-RAY DIFFRACTION Dmax: 124.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 53–205 Fragment:ECTODOMAIN, RESIDUES 53-205 R-SPONDIN-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246

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 14 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 3–155; UniProt 53–205 Author chain B; PDBConstruct 3–155; UniProt 53–205 Author chain C; PDBConstruct 3–155; UniProt 53–205 Author chain D; PDBConstruct 3–155; UniProt 53–205

R-SPONDIN-1

HOMO SAPIENS

UniProt Q2MKA7

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 31–145 Fragment:FURIN-LIKE DOMAIN, RESIDUES 31-145 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 1 (Q5SSZ7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 31–145 Fragment:FURIN-LIKE DOMAIN, RESIDUES 31-145 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 1 (Q5SSZ7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 31–145 Fragment:FURIN-LIKE DOMAIN, RESIDUES 31-145 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 1 (Q5SSZ7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 31–145 Fragment:FURIN-LIKE DOMAIN, RESIDUES 31-145 E3 UBIQUITIN-PROTEIN LIGASE ZNRF3 × 1 (Q5SSZ7) X-RAY DIFFRACTION X-ray crystallization conditions:0.2M SODIUM BROMIDE AND 20% W/V PEG 3350 Resolution 2.80 Å R-free 0.246

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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSPO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 3–117; UniProt 31–145 Author chain F; PDBConstruct 3–117; UniProt 31–145 Author chain G; PDBConstruct 3–117; UniProt 31–145 Author chain H; PDBConstruct 3–117; UniProt 31–145

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 4cdk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4cdk
Deposition date deposition_date2013-11-01
Structure title titleStructure of ZNRF3-RSPO1
Keywords keywordsLIGASE, WNT SIGNALING, ADULT STEM CELLS, E3 LIGASE, PROTEASE-ASSOCIATED DOMAIN, ZINC RING FINGER, LGR5, R-SPONDIN; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.49
Radius of gyration Rg (electron density) rg_electron33.48
Forward intensity I(0) i0216478000.00
Molecular weight molecular_weight113330.0 kDa
Excluded volume excluded_volume140320 ų
Envelope volume envelope_volume198670 ų
Hydration-shell volume shell_volume48858 ų
Envelope diameter envelope_diameter130.4
Shell Rg shell_rg40.47
Envelope Rg envelope_rg33.46
Shape Rg shape_rg33.42
Total Rg total_rg34.23
Total atoms total_atoms7896
Residues n_residues1040
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 dmax124.2
Rg (real space) rg_real34.39
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real2.1650e+08
I(0) uncertainty (real space) i0_real_error3.7010e+06
Rg (reciprocal space) rg_reciprocal34.45
I(0) (reciprocal space) i0_reciprocal216500000.0000
Solution quality estimate total_estimate0.8335
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.9
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.028
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23670000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.625; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4cdke_
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.3.9.1 — Growth factor receptor domain
Domain ID domain_idd4cdkf_
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.3.9.1 — Growth factor receptor domain
Domain ID domain_idd4cdkg_
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.3.9.1 — Growth factor receptor domain
Domain ID domain_idd4cdkh_
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.3.9.1 — Growth factor receptor domain

CATH v4.4 (8 domains)

Domain ID domain_id4cdkA00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4cdkB00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4cdkC00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4cdkD00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology30 — Glucose Oxidase; domain 1
Homologous superfamily homologous superfamily30
Domain ID domain_id4cdkE00
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_id4cdkF00
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_id4cdkG00
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_id4cdkH00
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)