1mih

A ROLE FOR CHEY GLU 89 IN CHEZ-MEDIATED DEPHOSPHORYLATION OF THE E. COLI CHEMOTAXIS RESPONSE REGULATOR CHEY

Method: X-RAY DIFFRACTION Dmax: 95.0 Å Quality: REASONABLE

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

Chemotaxis protein 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 0–128 Mutation:N59R MN MANGANESE (II) ION × 1 SO4 SULFATE ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;1.8 M Ammonium sulfate, 1 mM MnCl2, 10 mM NaF, 1 mM BeCl2, 5% glycerol, 10 mg/ml CheY N59R, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.277
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 0–128 Mutation:N59R MN MANGANESE (II) ION × 1 SO4 SULFATE ION × 2 BEF BERYLLIUM TRIFLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.4;293 K;1.8 M Ammonium sulfate, 1 mM MnCl2, 10 mM NaF, 1 mM BeCl2, 5% glycerol, 10 mg/ml CheY N59R, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.277

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 45 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 1–129; UniProt 0–128 Author chain B; PDBConstruct 1–129; UniProt 0–128

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 1mih

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mih
Deposition date deposition_date2002-08-23
Structure title titleA ROLE FOR CHEY GLU 89 IN CHEZ-MEDIATED DEPHOSPHORYLATION OF THE E. COLI CHEMOTAXIS RESPONSE REGULATOR CHEY
Keywords keywordsBacterial Chemotaxis, Response Regulator, Dephosphorylation, 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_guinier30.99
Radius of gyration Rg (electron density) rg_electron30.68
Forward intensity I(0) i013140100.00
Molecular weight molecular_weight28541.0 kDa
Excluded volume excluded_volume35793 ų
Envelope volume envelope_volume48876 ų
Hydration-shell volume shell_volume13396 ų
Envelope diameter envelope_diameter92.3
Shell Rg shell_rg37.54
Envelope Rg envelope_rg29.56
Shape Rg shape_rg30.69
Total Rg total_rg31.31
Total atoms total_atoms1989
Residues n_residues256
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 dmax95.0
Rg (real space) rg_real31.34
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real1.3140e+07
I(0) uncertainty (real space) i0_real_error2.0410e+05
Rg (reciprocal space) rg_reciprocal31.20
I(0) (reciprocal space) i0_reciprocal13140000.0000
Solution quality estimate total_estimate0.6191
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-1.322
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4182000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.024; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.089; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1miha_
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_idd1mihb_
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 (2 domains)

Domain ID domain_id1mihA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1mihB00
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)