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9yrs

E. Coli Glucokinase - K214Q

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Glucokinase

Escherichia coli

UniProt P0A6V8

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 1–321 Chain B； UniProt 1–321 Mutation：K214Q PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；297 K；100 mM MES / Sodium hydroxide pH 5.5, 100 mM Ammonium citrate dibasic, 20% (w/v) PEG 3350, 5% (v/v) 2-Propanol Resolution 2.70 Å R-free 0.190

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.

Other PDB Difference from Current Entry 9YRS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1Q18 Crystal structure of E.coli glucokinase (Glk) Deposited 2003-07-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–321（320 aa）
Chain B 2–321（320 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；20% PEG 4000, 0.1M Tris-HCl, 0.2M MgCl2, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.36 Å R-free 0.267
1SZ2 Crystal structure of E. coli glucokinase in complex with glucose Deposited 2004-04-02 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–321（320 aa） Fragment：glucokinase
Chain B 2–321（320 aa） Fragment：glucokinase
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) BGC beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 6000, MgCl2, Tris-HCl buffer, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.20 Å R-free 0.265

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLK_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–321； UniProt 1–321 Author chain B； PDBConstruct 1–321； UniProt 1–321

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 9yrs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yrs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yrs
Deposition date deposition_date2025-10-17
最后修订 last_revision2026-05-13
Structure title titleE. Coli Glucokinase - K214Q
Keywords keywordschemical modification, binding properties, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier27.91 Å
Radius of gyration Rg (electron density) rg_electron26.96 Å
Forward intensity I(0) i076020200.00
Molecular weight molecular_weight69326.0 kDa
Excluded volume excluded_volume87281 ų
Envelope volume envelope_volume106950 ų
Hydration-shell volume shell_volume33329 ų
Envelope diameter envelope_diameter90.1 Å
Shell Rg shell_rg34.26 Å
Envelope Rg envelope_rg27.02 Å
Shape Rg shape_rg26.94 Å
Total Rg total_rg27.81 Å
Total atoms total_atoms4884
Residues n_residues640
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax85.8 Å
Rg (real space) rg_real27.83 Å
Rg uncertainty (real space) rg_real_error0.55 Å
I(0) (real space) i0_real7.6020e+07
I(0) uncertainty (real space) i0_real_error1.1180e+06
Rg (reciprocal space) rg_reciprocal27.86 Å
I(0) (reciprocal space) i0_reciprocal76020000.0000
Solution quality estimate total_estimate0.9018
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6 Å
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.2850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18000000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.857
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)