5fgu

Structure of Sda1 nuclease apoprotein as an EGFP fixed-arm fusion

Method: X-RAY DIFFRACTION Dmax: 83.9 Å Quality: GOOD

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

Green fluorescent protein,Extracellular streptodornase D

Streptococcus pyogenes

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–229 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 6 EDO 1,2-ETHANEDIOL × 4 ACT ACETATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;Crystals were grown by mixing 0.25uL of protein (13.3mg/mL) with 0.25uL mother liquor (45mM Na cacodylate pH 6, 13.5mM magnesium sulfate, 1.53M ammonium sulfate), using sitting drop vapor diffusion Resolution 1.90 Å R-free 0.201
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–229 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 12 EDO 1,2-ETHANEDIOL × 8 ACT ACETATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;Crystals were grown by mixing 0.25uL of protein (13.3mg/mL) with 0.25uL mother liquor (45mM Na cacodylate pH 6, 13.5mM magnesium sulfate, 1.53M ammonium sulfate), using sitting drop vapor diffusion Resolution 1.90 Å R-free 0.201

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.

568 other PDB entries and 743 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–230; UniProt 1–229

Green fluorescent protein,Extracellular streptodornase D

Streptococcus pyogenes

UniProt Q675N6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 59–390 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 6 EDO 1,2-ETHANEDIOL × 4 ACT ACETATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;Crystals were grown by mixing 0.25uL of protein (13.3mg/mL) with 0.25uL mother liquor (45mM Na cacodylate pH 6, 13.5mM magnesium sulfate, 1.53M ammonium sulfate), using sitting drop vapor diffusion Resolution 1.90 Å R-free 0.201
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 59–390 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 12 EDO 1,2-ETHANEDIOL × 8 ACT ACETATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;Crystals were grown by mixing 0.25uL of protein (13.3mg/mL) with 0.25uL mother liquor (45mM Na cacodylate pH 6, 13.5mM magnesium sulfate, 1.53M ammonium sulfate), using sitting drop vapor diffusion Resolution 1.90 Å R-free 0.201

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.

1 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q675N6_STRPY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 234–565; UniProt 59–390

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 5fgu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5fgu
Deposition date deposition_date2015-12-21
Structure title titleStructure of Sda1 nuclease apoprotein as an EGFP fixed-arm fusion
Keywords keywordsbeta-beta-alpha metal finger nuclease, sequence nonspecific DNA binding, Metal binding protein, DNA binding protein, Metal binding; Metal binding, DNA binding protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.25
Radius of gyration Rg (electron density) rg_electron24.34
Forward intensity I(0) i052496900.00
Molecular weight molecular_weight54916.0 kDa
Excluded volume excluded_volume68082 ų
Envelope volume envelope_volume82808 ų
Hydration-shell volume shell_volume28323 ų
Envelope diameter envelope_diameter87.9
Shell Rg shell_rg31.66
Envelope Rg envelope_rg24.49
Shape Rg shape_rg24.33
Total Rg total_rg25.21
Total atoms total_atoms3860
Residues n_residues493
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 dmax83.9
Rg (real space) rg_real25.20
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real5.2500e+07
I(0) uncertainty (real space) i0_real_error6.7610e+05
Rg (reciprocal space) rg_reciprocal25.22
I(0) (reciprocal space) i0_reciprocal52500000.0000
Solution quality estimate total_estimate0.8906
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10960000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5fguA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (1)

9. Files and Curves (10)