3rvo

Structure of CheY-Mn2+ Complex with substitutions at 59 and 89: N59D E89Y

Method: X-RAY DIFFRACTION Dmax: 45.9 Å Quality: GOOD

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

Chemotaxis protein CheY

Escherichia coli

UniProt P0AE67

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–129 Mutation:N59D, E89Y MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;PEG 8000 30%, Na Cacodylate 100mM pH 6.0, Calcium Acetate 120mM, Glycerol 10% (v/v), 8.9 mg/mL CheY, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.55 Å R-free 0.185

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.

30 other PDB entries and 48 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 4–132; UniProt 1–129

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 3rvo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3rvo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3rvo
Deposition date deposition_date2011-05-06
Structure title titleStructure of CheY-Mn2+ Complex with substitutions at 59 and 89: N59D E89Y
Keywords keywords;two-component, signal transduction, response regulator, CheY, Beta-alpha protein, chemotaxis, CheZ, CheX, CheA, phosphorylation, 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_guinier14.95
Radius of gyration Rg (electron density) rg_electron13.43
Forward intensity I(0) i03887550.00
Molecular weight molecular_weight14183.0 kDa
Excluded volume excluded_volume17921 ų
Envelope volume envelope_volume19635 ų
Hydration-shell volume shell_volume12265 ų
Envelope diameter envelope_diameter44.6
Shell Rg shell_rg19.41
Envelope Rg envelope_rg13.71
Shape Rg shape_rg13.42
Total Rg total_rg14.77
Total atoms total_atoms2000
Residues n_residues129
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 dmax45.9
Rg (real space) rg_real14.81
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real3.8880e+06
I(0) uncertainty (real space) i0_real_error4.0710e+04
Rg (reciprocal space) rg_reciprocal14.82
I(0) (reciprocal space) i0_reciprocal3888000.0000
Solution quality estimate total_estimate0.8891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9
Skewness Skewness skewness-0.006
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha770200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3rvoa_
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 (1 domains)

Domain ID domain_id3rvoA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (1)

9. Files and Curves (10)