3amo

Time-resolved X-ray Crystal Structure Analysis of Enzymatic Reaction of Copper Amine Oxidase from Arthrobacter globiformis

Method: X-RAY DIFFRACTION Dmax: 106.8 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 1–638 Chain B; UniProt 1–638 Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 NA SODIUM ION × 2 GOL GLYCEROL × 97 X-RAY DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 6.8;293 K;20mM HEPES, 1.05M Sodium-potassium tartrate, pH 6.8, MICRODIALYSIS, temperature 293K Resolution 2.10 Å R-free 0.245

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–638; UniProt 1–638 Author chain B; PDBConstruct 1–638; UniProt 1–638

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 3amo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3amo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3amo
Deposition date deposition_date2010-08-20
Structure title titleTime-resolved X-ray Crystal Structure Analysis of Enzymatic Reaction of Copper Amine Oxidase from Arthrobacter globiformis
Keywords keywords;Amine Oxidase, Topaquinone, TPQ, Reaction Intermediate, Substrate Schiff-base, Product Schiff-base, Oxidoreductase, Phenylethylamine, TPQ Biogenesis ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.61
Radius of gyration Rg (electron density) rg_electron31.77
Forward intensity I(0) i0338400000.00
Molecular weight molecular_weight146670.0 kDa
Excluded volume excluded_volume182780 ų
Envelope volume envelope_volume209310 ų
Hydration-shell volume shell_volume52784 ų
Envelope diameter envelope_diameter114.2
Shell Rg shell_rg40.30
Envelope Rg envelope_rg32.01
Shape Rg shape_rg31.74
Total Rg total_rg32.47
Total atoms total_atoms10322
Residues n_residues1236
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 dmax106.8
Rg (real space) rg_real32.52
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real3.3840e+08
I(0) uncertainty (real space) i0_real_error5.0720e+06
Rg (reciprocal space) rg_reciprocal32.56
I(0) (reciprocal space) i0_reciprocal338400000.0000
Solution quality estimate total_estimate0.8750
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.2
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.227
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha101300000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd3amoa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd3amoa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd3amoa3
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain
Domain ID domain_idd3amob1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd3amob2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.2 — Amine oxidase N-terminal region
Family Family familyd.17.2.1 — Amine oxidase N-terminal region
Domain ID domain_idd3amob3
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.2 — Amine oxidase catalytic domain
Family Family familyb.30.2.1 — Amine oxidase catalytic domain

CATH v4.4 (6 domains)

Domain ID domain_id3amoA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id3amoA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id3amoA03
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_id3amoB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id3amoB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id3amoB03
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)