7wno

Crystallographic structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4 determined by only neutron diffraction data.

Method: NEUTRON DIFFRACTION Dmax: 93.7 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain X; UniProt 9–629 Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 NEUTRON DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;289 K;1.05-M potassium sodium (Na) tartrate in 25-mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer Resolution 1.72 Å R-free 0.257

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 7wno

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7wno
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7wno
Deposition date deposition_date2022-01-19
Structure title titleCrystallographic structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4 determined by only neutron diffraction data.
Keywords keywordstopaquinone, TPQ, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodNEUTRON DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.61
Radius of gyration Rg (electron density) rg_electron27.11
Forward intensity I(0) i0160602000.00
Molecular weight molecular_weight91313.0 kDa
Excluded volume excluded_volume108520 ų
Envelope volume envelope_volume149260 ų
Hydration-shell volume shell_volume42250 ų
Envelope diameter envelope_diameter100.8
Shell Rg shell_rg37.07
Envelope Rg envelope_rg28.92
Shape Rg shape_rg27.99
Total Rg total_rg25.42
Total atoms total_atoms12484
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 dmax93.7
Rg (real space) rg_real28.53
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.6060e+08
I(0) uncertainty (real space) i0_real_error2.6380e+06
Rg (reciprocal space) rg_reciprocal28.57
I(0) (reciprocal space) i0_reciprocal160600000.0000
Solution quality estimate total_estimate0.8889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22780000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)