1glc

CATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION

Method: X-RAY DIFFRACTION Dmax: 99.1 Å Quality: REASONABLE

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

GLUCOSE-SPECIFIC PROTEIN IIIGlc

Escherichia coli

UniProt P69783

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded GLYCEROL KINASE × 4 (P0A6F3) ZN ZINC ION × 4 MG MAGNESIUM ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded GLYCEROL KINASE × 2 (P0A6F3) ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 Å
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded GLYCEROL KINASE × 2 (P0A6F3) ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTGA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–168; UniProt 1–168

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–501 Not recorded GLUCOSE-SPECIFIC PROTEIN IIIGlc × 4 (P69783) ZN ZINC ION × 4 MG MAGNESIUM ION × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 Å
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–501 Not recorded GLUCOSE-SPECIFIC PROTEIN IIIGlc × 2 (P69783) ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 Å
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–501 Not recorded GLUCOSE-SPECIFIC PROTEIN IIIGlc × 2 (P69783) ZN ZINC ION × 2 MG MAGNESIUM ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 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 21 assemblies. Open the comparison page and filter oligomeric states

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

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 1glc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1glc
Deposition date deposition_date1994-03-07
Structure title titleCATION PROMOTED ASSOCIATION (CPA) OF A REGULATORY AND TARGET PROTEIN IS CONTROLLED BY PHOSPHORYLATION
Keywords keywordsPHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.90
Radius of gyration Rg (electron density) rg_electron27.74
Forward intensity I(0) i080262700.00
Molecular weight molecular_weight70332.0 kDa
Excluded volume excluded_volume87830 ų
Envelope volume envelope_volume104860 ų
Hydration-shell volume shell_volume32201 ų
Envelope diameter envelope_diameter105.0
Shell Rg shell_rg34.33
Envelope Rg envelope_rg28.50
Shape Rg shape_rg27.75
Total Rg total_rg28.31
Total atoms total_atoms4948
Residues n_residues650
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 dmax99.1
Rg (real space) rg_real28.09
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real8.0260e+07
I(0) uncertainty (real space) i0_real_error1.2880e+06
Rg (reciprocal space) rg_reciprocal28.03
I(0) (reciprocal space) i0_reciprocal80260000.0000
Solution quality estimate total_estimate0.6454
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.553
Kurtosis Kurtosis kurtosis-0.108
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43570000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.871; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1glcf_
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.3 — Duplicated hybrid motif
Family Family familyb.84.3.1 — Glucose permease-like
Domain ID domain_idd1glcg1
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_idd1glcg2
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 (3 domains)

Domain ID domain_id1glcF00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology70 — Glucose Permease (Domain IIA)
Homologous superfamily homologous superfamily10 — Glucose Permease (Domain IIA)
Domain ID domain_id1glcG01
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_id1glcG02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain

8. Citations (2)

9. Files and Curves (10)