1bo5

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.

Method: X-RAY DIFFRACTION Dmax: 114.2 Å Quality: GOOD

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

PROTEIN (GLYCEROL KINASE)

Escherichia coli

UniProt P0A6F3

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 O; UniProt 2–502 Chain Z; UniProt 2–502 Not recorded FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;PROTEIN CRYSTALLIZED FROM LIQUOR CONTAINING 1 M SODIUM CITRATE, 0.1 M HEPES PH 7.5, 1 MM BME. CRYO PROTECTION WAS ACHIEVED BY SOAKING CRYSTAL IN MOTHER LIQUOR CONTAINING 20% GLYCEROL FOR 4 HOURS. 20 MM FBP WAS ADDED TO THE CRYO PROTECTION IN THE SOAKING EXPERIMENT Resolution 3.20 Å
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain O; UniProt 2–502 Chain Z; UniProt 2–502 Not recorded FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 2 GOL GLYCEROL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;PROTEIN CRYSTALLIZED FROM LIQUOR CONTAINING 1 M SODIUM CITRATE, 0.1 M HEPES PH 7.5, 1 MM BME. CRYO PROTECTION WAS ACHIEVED BY SOAKING CRYSTAL IN MOTHER LIQUOR CONTAINING 20% GLYCEROL FOR 4 HOURS. 20 MM FBP WAS ADDED TO THE CRYO PROTECTION IN THE SOAKING EXPERIMENT Resolution 3.20 Å
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain O; UniProt 2–502 Not recorded FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;PROTEIN CRYSTALLIZED FROM LIQUOR CONTAINING 1 M SODIUM CITRATE, 0.1 M HEPES PH 7.5, 1 MM BME. CRYO PROTECTION WAS ACHIEVED BY SOAKING CRYSTAL IN MOTHER LIQUOR CONTAINING 20% GLYCEROL FOR 4 HOURS. 20 MM FBP WAS ADDED TO THE CRYO PROTECTION IN THE SOAKING EXPERIMENT Resolution 3.20 Å
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Z; UniProt 2–502 Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;PROTEIN CRYSTALLIZED FROM LIQUOR CONTAINING 1 M SODIUM CITRATE, 0.1 M HEPES PH 7.5, 1 MM BME. CRYO PROTECTION WAS ACHIEVED BY SOAKING CRYSTAL IN MOTHER LIQUOR CONTAINING 20% GLYCEROL FOR 4 HOURS. 20 MM FBP WAS ADDED TO THE CRYO PROTECTION IN THE SOAKING EXPERIMENT Resolution 3.20 Å

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLPK_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain O; PDBConstruct 1–501; UniProt 2–502 Author chain Z; PDBConstruct 1–501; UniProt 2–502

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 1bo5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bo5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bo5
Deposition date deposition_date1998-08-10
Structure title titleCRYSTAL STRUCTURE OF THE COMPLEX BETWEEN ESCHERICHIA COLI GLYCEROL KINASE AND THE ALLOSTERIC REGULATOR FRUCTOSE 1,6-BISPHOSPHATE.
Keywords keywordsKINASE, ALLOSTERIC REGULATION, FRUCTOSE BISPHOSPHATE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.60
Radius of gyration Rg (electron density) rg_electron39.48
Forward intensity I(0) i0187803000.00
Molecular weight molecular_weight110790.0 kDa
Excluded volume excluded_volume138080 ų
Envelope volume envelope_volume171430 ų
Hydration-shell volume shell_volume36629 ų
Envelope diameter envelope_diameter119.8
Shell Rg shell_rg44.44
Envelope Rg envelope_rg38.32
Shape Rg shape_rg39.47
Total Rg total_rg39.79
Total atoms total_atoms7798
Residues n_residues996
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 dmax114.2
Rg (real space) rg_real39.91
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.8780e+08
I(0) uncertainty (real space) i0_real_error3.4280e+06
Rg (reciprocal space) rg_reciprocal39.73
I(0) (reciprocal space) i0_reciprocal187800000.0000
Solution quality estimate total_estimate0.7618
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-1.026
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45360000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.666; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1bo5o1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.4 — Glycerol kinase
Domain ID domain_idd1bo5o2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.4 — Glycerol kinase
Domain ID domain_idd1bo5z1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.4 — Glycerol kinase
Domain ID domain_idd1bo5z2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.4 — Glycerol kinase

CATH v4.4 (4 domains)

Domain ID domain_id1bo5O01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id1bo5O02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id1bo5Z01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id1bo5Z02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain

8. Citations (1)

9. Files and Curves (10)