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1aoz

REFINED CRYSTAL STRUCTURE OF ASCORBATE OXIDASE AT 1.9 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 120.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ASCORBATE OXIDASE

Cucurbita pepo var. melopepo

UniProt P37064

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 1–552 Chain B； UniProt 1–552 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CU COPPER (II) ION × 5 C2O CU-O-CU LINKAGE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–552 Chain B； UniProt 1–552 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CU COPPER (II) ION × 10 C2O CU-O-CU LINKAGE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å

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.

Other PDB Difference from Current Entry 1AOZ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ASO X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CU COPPER (II) ION × 9 OH HYDROXIDE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1ASO X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CU COPPER (II) ION × 18 OH HYDROXIDE ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1ASP X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CU COPPER (II) ION × 9 OH HYDROXIDE ION × 2 PEO HYDROGEN PEROXIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.59 Å
1ASP X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CU COPPER (II) ION × 18 OH HYDROXIDE ION × 4 PEO HYDROGEN PEROXIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.59 Å
1ASQ X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CU COPPER (II) ION × 9 OH HYDROXIDE ION × 2 AZI AZIDE ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.32 Å
1ASQ X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS Deposited 1992-11-25 Different ligand/ion Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–552（552 aa）
Chain B 1–552（552 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CU COPPER (II) ION × 18 OH HYDROXIDE ION × 4 AZI AZIDE ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.32 Å

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASO_CUCPM
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–552； UniProt 1–552 Author chain B； PDBConstruct 1–552； UniProt 1–552

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 1aoz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aoz
Deposition date deposition_date1992-01-08
Structure title titleREFINED CRYSTAL STRUCTURE OF ASCORBATE OXIDASE AT 1.9 ANGSTROMS RESOLUTION
Keywords keywordsOXIDOREDUCTASE(OXYGEN ACCEPTOR); OXIDOREDUCTASE(OXYGEN ACCEPTOR)
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.87 Å
Radius of gyration Rg (electron density) rg_electron34.68 Å
Forward intensity I(0) i0235566000.00
Molecular weight molecular_weight124410.0 kDa
Excluded volume excluded_volume155520 ų
Envelope volume envelope_volume195090 ų
Hydration-shell volume shell_volume46747 ų
Envelope diameter envelope_diameter127.2 Å
Shell Rg shell_rg41.27 Å
Envelope Rg envelope_rg34.74 Å
Shape Rg shape_rg34.68 Å
Total Rg total_rg35.15 Å
Total atoms total_atoms8771
Residues n_residues1104
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax120.2 Å
Rg (real space) rg_real34.94 Å
Rg uncertainty (real space) rg_real_error1.03 Å
I(0) (real space) i0_real2.3560e+08
I(0) uncertainty (real space) i0_real_error3.5460e+06
Rg (reciprocal space) rg_reciprocal34.90 Å
I(0) (reciprocal space) i0_reciprocal235600000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.7 Å
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.413
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109700000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.783; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.969
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1aoza1
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1aoza2
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1aoza3
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1aozb1
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1aozb2
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1aozb3
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins

CATH v4.4 (6 domains)

Domain ID domain_id1aozA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aozA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aozA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aozB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aozB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aozB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
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8. Citations (2)

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9. Files and Curves (10)