5mxu

Structure of the Y503F mutant of vanillyl alcohol oxidase

Method: X-RAY DIFFRACTION Dmax: 98.2 Å Quality: GOOD

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

Vanillyl-alcohol oxidase

Penicillium simplicissimum

UniProt P56216

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 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

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.

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.

SAXS scattering curve SAXS Profile

SAXS profile for 5mxu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5mxu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5mxu
Deposition date deposition_date2017-01-24
Structure title titleStructure of the Y503F mutant of vanillyl alcohol oxidase
Keywords keywordsvanillyl alcohol oxidase, Y503F mutant, oxidoreductase; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.43
Radius of gyration Rg (electron density) rg_electron29.53
Forward intensity I(0) i0240118000.00
Molecular weight molecular_weight125160.0 kDa
Excluded volume excluded_volume156870 ų
Envelope volume envelope_volume181210 ų
Hydration-shell volume shell_volume48570 ų
Envelope diameter envelope_diameter99.3
Shell Rg shell_rg38.79
Envelope Rg envelope_rg29.83
Shape Rg shape_rg29.53
Total Rg total_rg30.27
Total atoms total_atoms8824
Residues n_residues1108
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 dmax98.2
Rg (real space) rg_real30.28
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real2.4010e+08
I(0) uncertainty (real space) i0_real_error3.4030e+06
Rg (reciprocal space) rg_reciprocal30.34
I(0) (reciprocal space) i0_reciprocal240100000.0000
Solution quality estimate total_estimate0.8900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha127500000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5mxua1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamilyd.145.1 — FAD-binding/transporter-associated domain-like
Family Family familyd.145.1.1 — FAD-linked oxidases, N-terminal domain
Domain ID domain_idd5mxua2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.32 — FAD-linked oxidases, C-terminal domain
Family Family familyd.58.32.1 — Vanillyl-alcohol oxidase-like
Domain ID domain_idd5mxub1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.145 — FAD-binding/transporter-associated domain-like
Superfamily Superfamily superfamilyd.145.1 — FAD-binding/transporter-associated domain-like
Family Family familyd.145.1.1 — FAD-linked oxidases, N-terminal domain
Domain ID domain_idd5mxub2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.32 — FAD-linked oxidases, C-terminal domain
Family Family familyd.58.32.1 — Vanillyl-alcohol oxidase-like

CATH v4.4 (8 domains)

Domain ID domain_id5mxuA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
Domain ID domain_id5mxuA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily10
Domain ID domain_id5mxuA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology462 — Vanillyl-alcohol Oxidase; Chain A, domain 3
Homologous superfamily homologous superfamily10 — FAD-linked oxidases, C-terminal domain
Domain ID domain_id5mxuA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology45 — Vanillyl-alcohol Oxidase; Chain A, domain 4
Homologous superfamily homologous superfamily10 — Vanillyl-alcohol Oxidase; Chain A, domain 4
Domain ID domain_id5mxuB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology43 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Homologous superfamily homologous superfamily10 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
Domain ID domain_id5mxuB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology465 — Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Homologous superfamily homologous superfamily10
Domain ID domain_id5mxuB03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology462 — Vanillyl-alcohol Oxidase; Chain A, domain 3
Homologous superfamily homologous superfamily10 — FAD-linked oxidases, C-terminal domain
Domain ID domain_id5mxuB04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology45 — Vanillyl-alcohol Oxidase; Chain A, domain 4
Homologous superfamily homologous superfamily10 — Vanillyl-alcohol Oxidase; Chain A, domain 4

8. Citations (1)

9. Files and Curves (10)