6l9c

Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4

Dmax: 89.6 Å Quality: GOOD

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

Phenylethylamine oxidase

Arthrobacter globiformis

UniProt P46881

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 X; UniProt 9–629 Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 1 NA SODIUM ION × 1 Experimental method not declared X-ray crystallization conditions:MICRODIALYSIS;pH 7.4;289 K;1.05M potassium-sodium tartrate, 25mM HEPES Resolution not provided

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.

105 other PDB entries and 143 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAOX_ARTGO
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–621; UniProt 9–629

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 6l9c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6l9c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6l9c
Deposition date deposition_date2019-11-08
Structure title titleNeutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4
Keywords keywordsCopper amine oxidase, topaquinone, TPQ, OXIDOREDUCTASE; OXIDOREDUCTASE

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

Radius of gyration Rg (Guinier) rg_guinier27.12
Radius of gyration Rg (electron density) rg_electron25.87
Forward intensity I(0) i079123500.00
Molecular weight molecular_weight69141.0 kDa
Excluded volume excluded_volume86211 ų
Envelope volume envelope_volume107700 ų
Hydration-shell volume shell_volume33886 ų
Envelope diameter envelope_diameter94.7
Shell Rg shell_rg33.88
Envelope Rg envelope_rg26.63
Shape Rg shape_rg25.84
Total Rg total_rg26.81
Total atoms total_atoms9392
Residues n_residues619
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 dmax89.6
Rg (real space) rg_real27.03
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real7.9120e+07
I(0) uncertainty (real space) i0_real_error1.1400e+06
Rg (reciprocal space) rg_reciprocal27.06
I(0) (reciprocal space) i0_reciprocal79130000.0000
Solution quality estimate total_estimate0.8868
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.294
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13340000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)