SAXSdb — 2vao

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1. Protein Identity and Related Structures Protein Identity & Related Structures

VANILLYL-ALCOHOL OXIDASE

OrganismNot specified

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–560 Chain B； UniProt 1–560	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 8	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.80 Å R-free 0.290

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 2VAO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AHU STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH P-CRESOL Deposited 1997-04-10	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	FAA N5-(4-HYDROXYBENZYL)FLAVIN-ADENINE DINUCLEOTIDE × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.70 Å R-free 0.290
1AHV STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 2-NITRO-P-CRESOL Deposited 1997-04-10	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 NCR 2-NITRO-P-CRESOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 3.10 Å R-free 0.240
1AHV STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 2-NITRO-P-CRESOL Deposited 1997-04-10	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NCR 2-NITRO-P-CRESOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 3.10 Å R-free 0.240
1AHZ STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 4-(1-HEPTENYL)PHENOL Deposited 1997-04-10	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	CL CHLORIDE ION × 8 FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 EPT HEPTANYL-P-PHENOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 3.30 Å R-free 0.260
1AHZ STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 4-(1-HEPTENYL)PHENOL Deposited 1997-04-10	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	CL CHLORIDE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EPT HEPTANYL-P-PHENOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 3.30 Å R-free 0.260
1DZN Asp170Ser mutant of vanillyl-alcohol oxidase Deposited 2000-03-05	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.80 Å R-free 0.291
1E0Y Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase Deposited 2000-04-11	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 FCR ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.75 Å R-free 0.287
1E8F STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM Deposited 2000-09-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 100 MM ACETATE BUFFER PH 4.6, 6% PEG4000	Resolution 2.90 Å R-free 0.312
1E8G STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL Deposited 2000-09-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 FCR ALPHA,ALPHA,ALPHA-TRIFLUORO-P-CRESOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；pH 4.60	Resolution 2.10 Å R-free 0.258
1E8H STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM COMPLEXED BY ADP Deposited 2000-09-20	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	ADP ADENOSINE-5'-DIPHOSPHATE × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.60 Å R-free 0.303
1QLT STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE Deposited 1999-09-16	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 ACT ACETATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.20 Å R-free 0.264
1QLU STRUCTURE OF THE H422A MUTANT VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL Deposited 1999-09-16	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.40 Å R-free 0.273
1VAO STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE Deposited 1997-04-10	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	ACT ACETATE ION × 8 CL CHLORIDE ION × 8 FAD FLAVIN-ADENINE DINUCLEOTIDE × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.50 Å R-free 0.290
1W1J STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant Deposited 2004-06-22	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.70 Å R-free 0.292
1W1K STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant Deposited 2004-06-22	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.55 Å R-free 0.272
1W1L STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant Deposited 2004-06-22	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 2.70 Å R-free 0.293
1W1M STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant Deposited 2004-06-22	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Mutation：YES Mutation：YES	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EUG 2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6	Resolution 3.00 Å R-free 0.307
5MXJ Structure of the Y108F mutant of vanillyl alcohol oxidase Deposited 2017-01-23	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 GOL GLYCEROL × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；PEG4000, sodium acetate	Resolution 2.80 Å R-free 0.259
5MXU Structure of the Y503F mutant of vanillyl alcohol oxidase Deposited 2017-01-24	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–560（560 aa） Chain B 1–560（560 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 8 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG4000, sodium acetate	Resolution 2.80 Å R-free 0.249

17 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VAOX_PENSI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–560； UniProt 1–560 Author chain B； PDBConstruct 1–560； UniProt 1–560

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2vao
Deposition date deposition_date	1997-04-10
Structure title title	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL
Keywords keywords	FLAVOENZYME, OXIDASE, CATALYSIS; FLAVOENZYME
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	30.23 Å
Radius of gyration Rg (electron density) rg_electron	29.39 Å
Forward intensity I(0) i0	242726000.00
Molecular weight molecular_weight	126420.0 kDa
Excluded volume excluded_volume	158670 Å³
Envelope volume envelope_volume	176850 Å³
Hydration-shell volume shell_volume	47779 Å³
Envelope diameter envelope_diameter	99.2 Å
Shell Rg shell_rg	38.55 Å
Envelope Rg envelope_rg	29.64 Å
Shape Rg shape_rg	29.38 Å
Total Rg total_rg	30.15 Å
Total atoms total_atoms	8910
Residues n_residues	1110
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	99.3 Å
Rg (real space) rg_real	30.08 Å
Rg uncertainty (real space) rg_real_error	0.47 Å
I(0) (real space) i0_real	2.4270e+08
I(0) uncertainty (real space) i0_real_error	3.2700e+06
Rg (reciprocal space) rg_reciprocal	30.15 Å
I(0) (reciprocal space) i0_reciprocal	242700000.0000
Solution quality estimate total_estimate	0.8853
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.221
Kurtosis Kurtosis kurtosis	-0.409
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	123000000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.838; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.993

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	VANILLYL-ALCOHOL OXIDASE
Molecular weight formula_weight	63107.1 kDa
EC 编号 ec_number	1.1.3.13
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	8948

MSKTQEFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISSKDQIVDGSYMKPTHTHDPHHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRNSGYGGAAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYLEANNLRDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLANGELLRTGMGALPDPKRPETMGLKPEDQPWSKIAHLFPYGFGPYIDGLFSQSNMGIVTKIGIWLMPNPRGYQSYLITLPKDGDLKQAVDIIRPLRLGMALQNVPTIRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYGALYGPEPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGIPTYDELKWIDWLPNGAHLFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFIGTFTVGMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRTHLAFMDQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSHVTWKL

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol
Molecular weight formula_weight	164.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	38

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2vaoa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.32 — FAD-linked oxidases, C-terminal domain
Family Family family	d.58.32.1 — Vanillyl-alcohol oxidase-like

Domain ID domain_id	d2vaoa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamily	d.145.1 — FAD-binding/transporter-associated domain-like
Family Family family	d.145.1.1 — FAD-linked oxidases, N-terminal domain

Domain ID domain_id	d2vaob1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.32 — FAD-linked oxidases, C-terminal domain
Family Family family	d.58.32.1 — Vanillyl-alcohol oxidase-like

Domain ID domain_id	d2vaob2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamily	d.145.1 — FAD-binding/transporter-associated domain-like
Family Family family	d.145.1.1 — FAD-linked oxidases, N-terminal domain

CATH v4.4 (8 domains)

Domain ID domain_id	2vaoA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily	10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2

Domain ID domain_id	2vaoA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2vaoA03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	462 — Vanillyl-alcohol Oxidase; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — FAD-linked oxidases, C-terminal domain

Domain ID domain_id	2vaoA04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	45 — Vanillyl-alcohol Oxidase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Vanillyl-alcohol Oxidase; Chain A, domain 4

Domain ID domain_id	2vaoB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily	10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2

Domain ID domain_id	2vaoB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2vaoB03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	462 — Vanillyl-alcohol Oxidase; Chain A, domain 3
Homologous superfamily homologous superfamily	10 — FAD-linked oxidases, C-terminal domain

Domain ID domain_id	2vaoB04
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	45 — Vanillyl-alcohol Oxidase; Chain A, domain 4
Homologous superfamily homologous superfamily	10 — Vanillyl-alcohol Oxidase; Chain A, domain 4

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8. Citations (1)

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Unit-cell length a length_a	128.380 Å
Unit-cell length b length_b	128.380 Å
Unit-cell length c length_c	130.190 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	I 4
Space-group number int_tables_number	79
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2150
R_work r_work	0.2140
R_free r_free	0.2900

fit	/app/data/saxs_computation/va/2vao/2vao.fit
pddf	/app/data/pr_computation/va/2vao/2vao.pr.out
profile	/app/data/saxs_computation/va/2vao/2vao.dat

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH ISOEUGENOL

1. Protein Identity and Related Structures Protein Identity & Related Structures

VANILLYL-ALCOHOL OXIDASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction