5b0i

Structure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside

Method: X-RAY DIFFRACTION Dmax: 132.8 Å Quality: GOOD

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

MoeN5,DNA-binding protein 7d

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

UniProt A0A010

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–260 Chain B; UniProt 1–260 Not recorded BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350, 5% Glycerol, 1% beta-octyl glucoside Resolution 2.26 Å R-free 0.229
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–260 Chain D; UniProt 1–260 Not recorded BOG octyl beta-D-glucopyranoside × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350, 5% Glycerol, 1% beta-octyl glucoside Resolution 2.26 Å R-free 0.229

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.

12 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A010_9ACTN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–274; UniProt 1–260 Author chain B; PDBConstruct 15–274; UniProt 1–260 Author chain C; PDBConstruct 15–274; UniProt 1–260 Author chain D; PDBConstruct 15–274; UniProt 1–260

MoeN5,DNA-binding protein 7d

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

UniProt P39476

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 Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–64 Chain B; UniProt 1–64 Not recorded BOG octyl beta-D-glucopyranoside × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350, 5% Glycerol, 1% beta-octyl glucoside Resolution 2.26 Å R-free 0.229
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–64 Chain D; UniProt 1–64 Not recorded BOG octyl beta-D-glucopyranoside × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.1;298 K;0.2M Li3-citrate, 0.3M NaCl, 25% PEG 3350, 5% Glycerol, 1% beta-octyl glucoside Resolution 2.26 Å R-free 0.229

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.

19 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DN72_SULSO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 280–343; UniProt 1–64 Author chain B; PDBConstruct 280–343; UniProt 1–64 Author chain C; PDBConstruct 280–343; UniProt 1–64 Author chain D; PDBConstruct 280–343; UniProt 1–64

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 5b0i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5b0i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5b0i
Deposition date deposition_date2015-10-30
Structure title titleStructure of MoeN5-Sso7d fusion protein in complex with beta-octyl glucoside
Keywords keywordsprenyltransferase, alpha-helical fold, fusion tag, ligand complex, TRANSFERASE, DNA BINDING PROTEIN; TRANSFERASE, DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.09
Radius of gyration Rg (electron density) rg_electron38.48
Forward intensity I(0) i0279368000.00
Molecular weight molecular_weight131190.0 kDa
Excluded volume excluded_volume162670 ų
Envelope volume envelope_volume213880 ų
Hydration-shell volume shell_volume47726 ų
Envelope diameter envelope_diameter142.8
Shell Rg shell_rg42.49
Envelope Rg envelope_rg39.53
Shape Rg shape_rg38.50
Total Rg total_rg38.67
Total atoms total_atoms9200
Residues n_residues1193
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 dmax132.8
Rg (real space) rg_real38.34
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.7940e+08
I(0) uncertainty (real space) i0_real_error5.5710e+06
Rg (reciprocal space) rg_reciprocal38.19
I(0) (reciprocal space) i0_reciprocal279300000.0000
Solution quality estimate total_estimate0.8552
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.9
Skewness Skewness skewness0.511
Kurtosis Kurtosis kurtosis-0.142
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48710000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.776

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id5b0iA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b0iB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b0iB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40
Domain ID domain_id5b0iC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b0iD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology600 — Farnesyl Diphosphate Synthase
Homologous superfamily homologous superfamily10 — Farnesyl Diphosphate Synthase
Domain ID domain_id5b0iD02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily40

8. Citations (1)

9. Files and Curves (10)