6wvd

Human JAGN1

Method: X-RAY DIFFRACTION Dmax: 106.7 Å Quality: REASONABLE

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

Green fluorescent protein, Protein jagunal homolog 1 chimera

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–144 Chain A; UniProt 146–231 Non-standard monomer:Yes (specific site not provided by mmCIF) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;295 K;30% PEG400, 0.1 M Li2SO4, 0.1M NaCl, 0.1 M Tris pH 8.0 Resolution 2.25 Å R-free 0.227

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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–142; UniProt 1–144 Author chain A; PDBConstruct 326–411; UniProt 146–231

Green fluorescent protein, Protein jagunal homolog 1 chimera

Aequorea victoria

UniProt Q8N5M9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–183 Non-standard monomer:Yes (specific site not provided by mmCIF) OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:LIPIDIC CUBIC PHASE;295 K;30% PEG400, 0.1 M Li2SO4, 0.1M NaCl, 0.1 M Tris pH 8.0 Resolution 2.25 Å R-free 0.227

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 JAGN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 143–325; UniProt 1–183

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 6wvd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wvd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wvd
Deposition date deposition_date2020-05-05
Structure title titleHuman JAGN1
Keywords keywordsJAGN1, Protein jagunal homolog 1, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.70
Radius of gyration Rg (electron density) rg_electron31.03
Forward intensity I(0) i031252100.00
Molecular weight molecular_weight45761.0 kDa
Excluded volume excluded_volume58083 ų
Envelope volume envelope_volume74305 ų
Hydration-shell volume shell_volume21594 ų
Envelope diameter envelope_diameter105.4
Shell Rg shell_rg34.96
Envelope Rg envelope_rg31.36
Shape Rg shape_rg31.04
Total Rg total_rg31.37
Total atoms total_atoms3229
Residues n_residues397
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 dmax106.7
Rg (real space) rg_real31.24
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.1250e+07
I(0) uncertainty (real space) i0_real_error5.8600e+05
Rg (reciprocal space) rg_reciprocal31.01
I(0) (reciprocal space) i0_reciprocal31250000.0000
Solution quality estimate total_estimate0.7411
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.604
Kurtosis Kurtosis kurtosis-0.501
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3465000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.510; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.268; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)