1cye

THREE DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE METHODS

Method: SOLUTION NMR Dmax: 45.2 Å Quality: GOOD

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

CHEY

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–128 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 46 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 3–129; UniProt 2–128

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 1cye

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cye
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cye
Deposition date deposition_date1994-10-21
Structure title titleTHREE DIMENSIONAL STRUCTURE OF CHEMOTACTIC CHE Y PROTEIN IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE METHODS
Keywords keywordsSIGNAL TRANSDUCTION; SIGNAL TRANSDUCTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.66
Radius of gyration Rg (electron density) rg_electron13.30
Forward intensity I(0) i01054260000.00
Molecular weight molecular_weight282710.0 kDa
Excluded volume excluded_volume356990 ų
Envelope volume envelope_volume26846 ų
Hydration-shell volume shell_volume14893 ų
Envelope diameter envelope_diameter50.5
Shell Rg shell_rg21.23
Envelope Rg envelope_rg15.24
Shape Rg shape_rg13.28
Total Rg total_rg13.49
Total atoms total_atoms24200
Residues n_residues2580
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 dmax45.2
Rg (real space) rg_real13.52
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.0540e+09
I(0) uncertainty (real space) i0_real_error1.2160e+07
Rg (reciprocal space) rg_reciprocal13.53
I(0) (reciprocal space) i0_reciprocal1054000000.0000
Solution quality estimate total_estimate0.8583
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness-0.104
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha315800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.722; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cyea_
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_id1cyeA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (2)

9. Files and Curves (10)