1f4v

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

Method: X-RAY DIFFRACTION Dmax: 97.6 Å Quality: REASONABLE

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

CHEMOTAXIS CHEY PROTEIN

Escherichia coli

UniProt P06143

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–128 Not recorded FLAGELLAR MOTOR SWITCH PROTEIN × 1 (P06974) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–128 Not recorded FLAGELLAR MOTOR SWITCH PROTEIN × 1 (P06974) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–128 Not recorded FLAGELLAR MOTOR SWITCH PROTEIN × 1 (P06974) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258

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.

27 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHEY_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–128; UniProt 1–128 Author chain B; PDBConstruct 1–128; UniProt 1–128 Author chain C; PDBConstruct 1–128; UniProt 1–128

FLAGELLAR MOTOR SWITCH PROTEIN

OrganismNot specified

UniProt P06974

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–16 Fragment:N-TERMINUS CHEMOTAXIS CHEY PROTEIN × 1 (P06143) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–16 Fragment:N-TERMINUS CHEMOTAXIS CHEY PROTEIN × 1 (P06143) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–16 Fragment:N-TERMINUS CHEMOTAXIS CHEY PROTEIN × 1 (P06143) MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;298 K;ammonium sulfate, glycerol, Tris, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.22 Å R-free 0.258

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIM_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–16; UniProt 1–16 Author chain E; PDBConstruct 1–16; UniProt 1–16 Author chain F; PDBConstruct 1–16; UniProt 1–16

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 1f4v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f4v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f4v
Deposition date deposition_date2000-06-10
Structure title titleCRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM
Keywords keywordsresponse regulator, peptide-protein complex, bacterial signal transduction, BeF3, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.31
Radius of gyration Rg (electron density) rg_electron27.71
Forward intensity I(0) i034715500.00
Molecular weight molecular_weight46736.0 kDa
Excluded volume excluded_volume58939 ų
Envelope volume envelope_volume71898 ų
Hydration-shell volume shell_volume23162 ų
Envelope diameter envelope_diameter102.3
Shell Rg shell_rg32.78
Envelope Rg envelope_rg27.68
Shape Rg shape_rg27.68
Total Rg total_rg28.32
Total atoms total_atoms3273
Residues n_residues426
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 dmax97.6
Rg (real space) rg_real28.55
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real3.4720e+07
I(0) uncertainty (real space) i0_real_error5.2340e+05
Rg (reciprocal space) rg_reciprocal28.48
I(0) (reciprocal space) i0_reciprocal34710000.0000
Solution quality estimate total_estimate0.6536
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.427
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13420000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.723; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.630; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1f4va_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.1 — CheY-like
Family Family familyc.23.1.1 — CheY-related
Domain ID domain_idd1f4vb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.1 — CheY-like
Family Family familyc.23.1.1 — CheY-related
Domain ID domain_idd1f4vc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.1 — CheY-like
Family Family familyc.23.1.1 — CheY-related

CATH v4.4 (3 domains)

Domain ID domain_id1f4vA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1f4vB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1f4vC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (4)

9. Files and Curves (10)