1w6g

AGAO holoenzyme at 1.55 angstroms

Method: X-RAY DIFFRACTION Dmax: 91.7 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 3–638 Fragment:AGAO HOLOENZYME, RESIDUES 3-638 Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 4 NA SODIUM ION × 2 SO4 SULFATE ION × 4 GOL GLYCEROL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;THE CRYSTAL WAS GROWN BY HANGING DROP DIFFUSION AT 293K. THE RESERVOIR WAS 1.2M (NH4)2SO4, 12% DIOXANE, 0.1M MES PH6.5. THE DROP CONTAINED 1.5MICROLITER OF 11.7 MG/ML PROTEIN, 0.05M HEPES PH7.0, PLUS 1.5 MICROLITER OF RESERVOIR SOLUTION. A CRYSTAL WAS CRYOPROTECTED BY GRADUAL INCREMENTAL SOAKING IN RESERVOIR SOLUTION MIXED WITH GLYCEROL. THE CONCENTRATION OF GLYCEROL WAS INCREASED FROM 0 TO 30% IN 2-3% INCREMENTS DURING 2 HOURS. THE CRYSTAL WAS THEN FROZEN IN THE CRYOSTREAM., pH 7.00 Resolution 1.55 Å R-free 0.188

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 A; PDBConstruct 1–636; UniProt 3–638

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 1w6g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w6g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1w6g
Deposition date deposition_date2004-08-18
Structure title titleAGAO holoenzyme at 1.55 angstroms
Keywords keywordsAMINE OXIDASE, ARTHROBACTER GLOBIFORMIS, COPPER CONTAINING, METAL-BINDING, OXIDOREDUCTASE, TPQ, QUINONE, HOLOENZYME; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.16
Radius of gyration Rg (electron density) rg_electron25.92
Forward intensity I(0) i082556700.00
Molecular weight molecular_weight69597.0 kDa
Excluded volume excluded_volume86387 ų
Envelope volume envelope_volume107830 ų
Hydration-shell volume shell_volume34008 ų
Envelope diameter envelope_diameter95.2
Shell Rg shell_rg33.80
Envelope Rg envelope_rg26.49
Shape Rg shape_rg25.88
Total Rg total_rg26.86
Total atoms total_atoms9401
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 dmax91.7
Rg (real space) rg_real27.07
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real8.2560e+07
I(0) uncertainty (real space) i0_real_error1.2640e+06
Rg (reciprocal space) rg_reciprocal27.10
I(0) (reciprocal space) i0_reciprocal82560000.0000
Solution quality estimate total_estimate0.8027
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14120000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1w6ga1
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_idd1w6ga2
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_idd1w6ga3
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

CATH v4.4 (3 domains)

Domain ID domain_id1w6gA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id1w6gA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily40
Domain ID domain_id1w6gA03
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 (2)

9. Files and Curves (10)