10sr

Crystal structure of Guanylate Kinase from Burkholderia thailandensis in complex with GMP

Method: X-RAY DIFFRACTION Dmax: 139.2 Å Quality: GOOD

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

Guanylate kinase

Burkholderia thailandensis E264

UniProt Q2SY72

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 18–224 Chain B; UniProt 18–224 Not recorded 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;1.6M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6. ButhA.01463.a.A1.PB00147 at 21.6 mg/mL. Cocrystallization with 2 mM GMP. plate Liu-S197 H3, Puck: PSL-1813, Cryo: 4.0M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6 Resolution 3.02 Å R-free 0.249
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 18–224 Chain D; UniProt 18–224 Not recorded 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;1.6M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6. ButhA.01463.a.A1.PB00147 at 21.6 mg/mL. Cocrystallization with 2 mM GMP. plate Liu-S197 H3, Puck: PSL-1813, Cryo: 4.0M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6 Resolution 3.02 Å R-free 0.249
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 18–224 Chain F; UniProt 18–224 Not recorded 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;1.6M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6. ButhA.01463.a.A1.PB00147 at 21.6 mg/mL. Cocrystallization with 2 mM GMP. plate Liu-S197 H3, Puck: PSL-1813, Cryo: 4.0M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6 Resolution 3.02 Å R-free 0.249
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 18–224 Chain H; UniProt 18–224 Not recorded 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;291 K;1.6M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6. ButhA.01463.a.A1.PB00147 at 21.6 mg/mL. Cocrystallization with 2 mM GMP. plate Liu-S197 H3, Puck: PSL-1813, Cryo: 4.0M Sodium Formate, 0.1M Acetate/acidic acid, pH 4.6 Resolution 3.02 Å R-free 0.249

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 KGUA_BURTA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–214; UniProt 18–224 Author chain B; PDBConstruct 8–214; UniProt 18–224 Author chain C; PDBConstruct 8–214; UniProt 18–224 Author chain D; PDBConstruct 8–214; UniProt 18–224 Author chain E; PDBConstruct 8–214; UniProt 18–224 Author chain F; PDBConstruct 8–214; UniProt 18–224 Author chain G; PDBConstruct 8–214; UniProt 18–224 Author chain H; PDBConstruct 8–214; UniProt 18–224

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 10sr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10sr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10sr
Deposition date deposition_date2026-02-06
最后修订 last_revision2026-02-18
Structure title titleCrystal structure of Guanylate Kinase from Burkholderia thailandensis in complex with GMP
Keywords keywordsSSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE, Guanylate Kinase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier46.05
Radius of gyration Rg (electron density) rg_electron45.28
Forward intensity I(0) i0509900000.00
Molecular weight molecular_weight183110.0 kDa
Excluded volume excluded_volume227650 ų
Envelope volume envelope_volume351290 ų
Hydration-shell volume shell_volume63844 ų
Envelope diameter envelope_diameter141.0
Shell Rg shell_rg52.56
Envelope Rg envelope_rg42.60
Shape Rg shape_rg45.27
Total Rg total_rg45.65
Total atoms total_atoms12936
Residues n_residues1630
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 dmax139.2
Rg (real space) rg_real45.76
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real5.0990e+08
I(0) uncertainty (real space) i0_real_error9.0230e+06
Rg (reciprocal space) rg_reciprocal46.05
I(0) (reciprocal space) i0_reciprocal510100000.0000
Solution quality estimate total_estimate0.8296
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.6
Skewness Skewness skewness-0.079
Kurtosis Kurtosis kurtosis-0.823
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29370000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)