5efw

Crystal structure of LOV2-Zdk1 - the complex of oat LOV2 and the affibody protein Zdark1

Method: X-RAY DIFFRACTION Dmax: 74.6 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 404–546 Fragment:UNP residues 404-546 Mutation:C450A Z-dark, a small protein based on the Z domain affibody × 2 FMN FLAVIN MONONUCLEOTIDE × 1 SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 3.5;293.15 K;2 M ammonium sulfate, 0.1 M sodium citrate pH 3.5 Resolution 2.10 Å R-free 0.257

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 3–145; 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 5efw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5efw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5efw
Deposition date deposition_date2015-10-26
Structure title titleCrystal structure of LOV2-Zdk1 - the complex of oat LOV2 and the affibody protein Zdark1
Keywords keywordsLOV domain, photoreceptor, affibody, optogenetic tool, signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.50
Radius of gyration Rg (electron density) rg_electron19.46
Forward intensity I(0) i015733000.00
Molecular weight molecular_weight28669.0 kDa
Excluded volume excluded_volume35449 ų
Envelope volume envelope_volume42299 ų
Hydration-shell volume shell_volume18685 ų
Envelope diameter envelope_diameter78.2
Shell Rg shell_rg25.63
Envelope Rg envelope_rg20.02
Shape Rg shape_rg19.40
Total Rg total_rg20.52
Total atoms total_atoms2012
Residues n_residues245
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 dmax74.6
Rg (real space) rg_real20.54
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.5730e+07
I(0) uncertainty (real space) i0_real_error2.3020e+05
Rg (reciprocal space) rg_reciprocal20.53
I(0) (reciprocal space) i0_reciprocal15730000.0000
Solution quality estimate total_estimate0.7513
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.486
Kurtosis Kurtosis kurtosis0.070
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3876000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.607; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5efwb_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family familya.8.1.1 — Immunoglobulin-binding protein A modules
Domain ID domain_idd5efwc_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family familya.8.1.1 — Immunoglobulin-binding protein A modules

CATH v4.4 (3 domains)

Domain ID domain_id5efwA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id5efwB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id5efwC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C

8. Citations (1)

9. Files and Curves (10)