1qlt

STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE

Method: X-RAY DIFFRACTION Dmax: 93.8 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 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

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 1qlt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qlt
Deposition date deposition_date1999-09-16
Structure title titleSTRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE
Keywords keywordsOXIDOREDUCTASE, FLAVOPROTEIN, METHANOL UTILIZATION, PEROXISOME, FLAVOENZYME, OXIDASE, CATALYSIS; FLAVOENZYME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.24
Radius of gyration Rg (electron density) rg_electron29.40
Forward intensity I(0) i0237761000.00
Molecular weight molecular_weight124970.0 kDa
Excluded volume excluded_volume156850 ų
Envelope volume envelope_volume179170 ų
Hydration-shell volume shell_volume48236 ų
Envelope diameter envelope_diameter99.3
Shell Rg shell_rg38.70
Envelope Rg envelope_rg29.69
Shape Rg shape_rg29.39
Total Rg total_rg30.17
Total atoms total_atoms8806
Residues n_residues1100
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 dmax93.8
Rg (real space) rg_real30.09
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.3780e+08
I(0) uncertainty (real space) i0_real_error3.4390e+06
Rg (reciprocal space) rg_reciprocal30.16
I(0) (reciprocal space) i0_reciprocal237800000.0000
Solution quality estimate total_estimate0.8981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.9
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha117000000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.934

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_idd1qlta1
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_idd1qlta2
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_idd1qltb1
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_idd1qltb2
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

CATH v4.4 (8 domains)

Domain ID domain_id1qltA01
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_id1qltA02
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_id1qltA03
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_id1qltA04
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_id1qltB01
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_id1qltB02
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_id1qltB03
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_id1qltB04
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 (2)

9. Files and Curves (10)