4c8w

Xenopus RSPO2 Fu1-Fu2 crystal form II

Method: X-RAY DIFFRACTION Dmax: 71.8 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain I; UniProt 35–144 Fragment:FU1-FU2, RESIDUES 35-144 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.313
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain J; UniProt 35–144 Fragment:FU1-FU2, RESIDUES 35-144 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.10 Å R-free 0.313

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 1
Chains and sequence ranges Author chain I; PDBConstruct 4–113; UniProt 35–144 Author chain J; 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 4c8w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c8w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c8w
Deposition date deposition_date2013-10-01
Structure title titleXenopus RSPO2 Fu1-Fu2 crystal form II
Keywords keywordsSIGNALING PROTEIN, WNT, ZNRF3, RNF43, LGR4, LGR5, LGR6, RSPO, R-SPO, RSPO1, RSPO3, RSPO4, RECEPTOR, MEMBRANE, SIGNALLING; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.98
Radius of gyration Rg (electron density) rg_electron22.43
Forward intensity I(0) i010736900.00
Molecular weight molecular_weight22488.0 kDa
Excluded volume excluded_volume27228 ų
Envelope volume envelope_volume37251 ų
Hydration-shell volume shell_volume15001 ų
Envelope diameter envelope_diameter74.5
Shell Rg shell_rg27.46
Envelope Rg envelope_rg22.35
Shape Rg shape_rg22.42
Total Rg total_rg23.16
Total atoms total_atoms1549
Residues n_residues208
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 dmax71.8
Rg (real space) rg_real23.00
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.0740e+07
I(0) uncertainty (real space) i0_real_error1.7080e+05
Rg (reciprocal space) rg_reciprocal23.00
I(0) (reciprocal space) i0_reciprocal10740000.0000
Solution quality estimate total_estimate0.7467
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.2
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.793
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha529700.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.976; Stabil: 1.000; Sysdev: 0.307; Positv: 1.000; Valcen: 0.881; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4c8wi_
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_idd4c8wj_
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 (2 domains)

Domain ID domain_id4c8wI00
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_id4c8wJ00
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)