1bwf

ESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION

Method: X-RAY DIFFRACTION Dmax: 113.9 Å Quality: GOOD

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

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 1–501 Chain Y; UniProt 1–501 Mutation:S58W MG MAGNESIUM ION × 2 ATF PHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 3.00 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 23 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 1–501 Author chain Y; 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 1bwf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bwf
Deposition date deposition_date1998-09-23
Structure title titleESCHERICHIA COLI GLYCEROL KINASE MUTANT WITH BOUND ATP ANALOG SHOWING SUBSTANTIAL DOMAIN MOTION
Keywords keywordsTRANSFERASE, KINASE, DOMAIN MOTION, ALLOSTERIC REGULATION HYDROLASE, LIPID DEGRADATION, PLATELET FACTOR; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.80
Radius of gyration Rg (electron density) rg_electron34.66
Forward intensity I(0) i0200333000.00
Molecular weight molecular_weight112370.0 kDa
Excluded volume excluded_volume139700 ų
Envelope volume envelope_volume163240 ų
Hydration-shell volume shell_volume40683 ų
Envelope diameter envelope_diameter115.8
Shell Rg shell_rg39.91
Envelope Rg envelope_rg34.61
Shape Rg shape_rg34.65
Total Rg total_rg35.03
Total atoms total_atoms7900
Residues n_residues988
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 dmax113.9
Rg (real space) rg_real35.00
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.0030e+08
I(0) uncertainty (real space) i0_real_error3.4520e+06
Rg (reciprocal space) rg_reciprocal34.88
I(0) (reciprocal space) i0_reciprocal200300000.0000
Solution quality estimate total_estimate0.7870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis-0.584
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125700000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.881; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1bwfo1
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_idd1bwfo2
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_idd1bwfy1
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_idd1bwfy2
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_id1bwfO01
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_id1bwfO02
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_id1bwfY01
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_id1bwfY02
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)