5zpm

Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by phenylethylamine at pH 7 at 288 K (2)

Method: X-RAY DIFFRACTION Dmax: 140.7 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 A; UniProt 9–628 Non-standard monomer:Yes (specific site not provided by mmCIF) NA SODIUM ION × 4 EDO 1,2-ETHANEDIOL × 2 CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 7.4;289 K;1.05M potassium-sodium tartrate, 25mM HEPES Resolution 1.65 Å R-free 0.171
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 9–628 Non-standard monomer:Yes (specific site not provided by mmCIF) NA SODIUM ION × 2 EDO 1,2-ETHANEDIOL × 4 CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 7.4;289 K;1.05M potassium-sodium tartrate, 25mM HEPES Resolution 1.65 Å R-free 0.171

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 142 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 A; PDBConstruct 1–620; UniProt 9–628 Author chain B; PDBConstruct 1–620; UniProt 9–628

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 5zpm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5zpm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5zpm
Deposition date deposition_date2018-04-16
Structure title titleCopper amine oxidase from Arthrobacter globiformis anaerobically reduced by phenylethylamine at pH 7 at 288 K (2)
Keywords keywordsCOPPER AMINE OXIDASE, TOPAQUINONE, TPQ, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.07
Radius of gyration Rg (electron density) rg_electron37.53
Forward intensity I(0) i0297286000.00
Molecular weight molecular_weight138210.0 kDa
Excluded volume excluded_volume171980 ų
Envelope volume envelope_volume230210 ų
Hydration-shell volume shell_volume50676 ų
Envelope diameter envelope_diameter150.1
Shell Rg shell_rg43.43
Envelope Rg envelope_rg38.26
Shape Rg shape_rg37.52
Total Rg total_rg37.93
Total atoms total_atoms9771
Residues n_residues1238
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 dmax140.7
Rg (real space) rg_real38.16
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real2.9730e+08
I(0) uncertainty (real space) i0_real_error5.7760e+06
Rg (reciprocal space) rg_reciprocal38.10
I(0) (reciprocal space) i0_reciprocal297300000.0000
Solution quality estimate total_estimate0.8451
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.2
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65380000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.701; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id5zpmA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id5zpmA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id5zpmA03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain
Domain ID domain_id5zpmB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id5zpmB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id5zpmB03
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily20 — Copper amine oxidase, catalytic domain

8. Citations (1)

9. Files and Curves (10)