8tzp

Structure of human Wnt7a bound to WLS and RECK

Method: ELECTRON MICROSCOPY Dmax: 122.6 Å Quality: GOOD

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

Protein Wnt-7a

Homo sapiens

UniProt O00755

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–349 Not recorded Protein wntless homolog × 1 (Q5T9L3) Reversion-inducing cysteine-rich protein with Kazal motifs × 1 (O95980) PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WNT7A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–349; UniProt 1–349

Protein wntless homolog

Homo sapiens

UniProt Q5T9L3

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–541 Not recorded Protein Wnt-7a × 1 (O00755) Reversion-inducing cysteine-rich protein with Kazal motifs × 1 (O95980) PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 Å

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WLS_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–541; UniProt 1–541

Reversion-inducing cysteine-rich protein with Kazal motifs

Homo sapiens

UniProt O95980

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–971 Not recorded Protein Wnt-7a × 1 (O00755) Protein wntless homolog × 1 (Q5T9L3) PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RECK_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–971; UniProt 1–971

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 8tzp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tzp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tzp
Deposition date deposition_date2023-08-27
Structure title titleStructure of human Wnt7a bound to WLS and RECK
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.26
Radius of gyration Rg (electron density) rg_electron35.03
Forward intensity I(0) i0144090000.00
Molecular weight molecular_weight98751.0 kDa
Excluded volume excluded_volume124610 ų
Envelope volume envelope_volume166190 ų
Hydration-shell volume shell_volume40971 ų
Envelope diameter envelope_diameter123.9
Shell Rg shell_rg39.78
Envelope Rg envelope_rg35.08
Shape Rg shape_rg34.99
Total Rg total_rg35.56
Total atoms total_atoms6920
Residues n_residues859
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 dmax122.6
Rg (real space) rg_real35.49
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.4410e+08
I(0) uncertainty (real space) i0_real_error2.5630e+06
Rg (reciprocal space) rg_reciprocal35.35
I(0) (reciprocal space) i0_reciprocal144100000.0000
Solution quality estimate total_estimate0.8494
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15970000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)