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1asp

X-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS

Method: X-RAY DIFFRACTION Dmax: 121.7 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 × 9 OH HYDROXIDE ION × 2 PEO HYDROGEN PEROXIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.59 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 × 18 OH HYDROXIDE ION × 4 PEO HYDROGEN PEROXIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.59 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 1ASP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AOZ REFINED CRYSTAL STRUCTURE OF ASCORBATE OXIDASE AT 1.9 ANGSTROMS RESOLUTION Deposited 1992-01-08 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 × 5 C2O CU-O-CU LINKAGE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å
1AOZ REFINED CRYSTAL STRUCTURE OF ASCORBATE OXIDASE AT 1.9 ANGSTROMS RESOLUTION Deposited 1992-01-08 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 × 10 C2O CU-O-CU LINKAGE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 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 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
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 1asp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1asp
Deposition date deposition_date1992-11-25
Structure title titleX-RAY STRUCTURES AND MECHANISTIC IMPLICATIONS OF THREE FUNCTIONAL DERIVATIVES OF ASCORBATE OXIDASE FROM ZUCCHINI: REDUCED-, PEROXIDE-, AND AZIDE-FORMS
Keywords keywordsOXIDOREDUCTASE; OXIDOREDUCTASE
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_electron34.69 Å
Forward intensity I(0) i0236069000.00
Molecular weight molecular_weight124480.0 kDa
Excluded volume excluded_volume155590 ų
Envelope volume envelope_volume194450 ų
Hydration-shell volume shell_volume46637 ų
Envelope diameter envelope_diameter127.2 Å
Shell Rg shell_rg41.21 Å
Envelope Rg envelope_rg34.74 Å
Shape Rg shape_rg34.69 Å
Total Rg total_rg35.15 Å
Total atoms total_atoms8775
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 dmax121.7 Å
Rg (real space) rg_real34.95 Å
Rg uncertainty (real space) rg_real_error1.08 Å
I(0) (real space) i0_real2.3610e+08
I(0) uncertainty (real space) i0_real_error3.8810e+06
Rg (reciprocal space) rg_reciprocal34.90 Å
I(0) (reciprocal space) i0_reciprocal236100000.0000
Solution quality estimate total_estimate0.8606
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.2 Å
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110400000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.759; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.966
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1aspa1
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_idd1aspa2
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_idd1aspa3
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_idd1aspb1
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_idd1aspb2
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_idd1aspb3
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_id1aspA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aspA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aspA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aspB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aspB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1aspB03
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 (3)

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9. Files and Curves (10)