2v1a

N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal transduction (room temperature (293K) dark structure of LOV2 (404-546))

Method: X-RAY DIFFRACTION Dmax: 51.9 Å Quality: GOOD

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

NPH1-1

AVENA SATIVA

UniProt O49003

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 404–546 Fragment:LIGHT, OXYGEN, VOLTAGE DOMAIN, RESIDUES 404-546 FMN FLAVIN MONONUCLEOTIDE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP Resolution 1.65 Å R-free 0.195

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O49003_AVESA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–144; UniProt 404–546

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 2v1a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2v1a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2v1a
Deposition date deposition_date2007-05-22
Structure title titleN- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal transduction (room temperature (293K) dark structure of LOV2 (404-546))
Keywords keywords;LOV2, KINASE, TRANSFERASE, ATP-BINDING, AVENA SATIVA, SERINE/THREONINE-PROTEIN KINASE, LIGHT-INDUCED SIGNAL TRANSDUCTION, PHOTOTROPIN1, NUCLEOTIDE-BINDING ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.09
Radius of gyration Rg (electron density) rg_electron14.72
Forward intensity I(0) i05940910.00
Molecular weight molecular_weight17281.0 kDa
Excluded volume excluded_volume21529 ų
Envelope volume envelope_volume24446 ų
Hydration-shell volume shell_volume13889 ų
Envelope diameter envelope_diameter51.3
Shell Rg shell_rg20.78
Envelope Rg envelope_rg15.14
Shape Rg shape_rg14.68
Total Rg total_rg15.97
Total atoms total_atoms1216
Residues n_residues144
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 dmax51.9
Rg (real space) rg_real15.97
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real5.9410e+06
I(0) uncertainty (real space) i0_real_error6.5260e+04
Rg (reciprocal space) rg_reciprocal15.98
I(0) (reciprocal space) i0_reciprocal5941000.0000
Solution quality estimate total_estimate0.8810
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1337000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2v1aA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain

8. Citations (1)

9. Files and Curves (10)