1vlz

UNCOUPLED PHOSPHORYLATION AND ACTIVATION IN BACTERIAL CHEMOTAXIS: THE 2.1 ANGSTROM STRUCTURE OF A THREONINE TO ISOLEUCINE MUTANT AT POSITION 87 OF CHEY

Method: X-RAY DIFFRACTION Dmax: 68.2 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–128 Chain B; UniProt 1–128 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.05 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.

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 1–128; UniProt 1–128 Author chain B; PDBConstruct 1–128; UniProt 1–128

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 1vlz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1vlz
Deposition date deposition_date1995-04-21
Structure title titleUNCOUPLED PHOSPHORYLATION AND ACTIVATION IN BACTERIAL CHEMOTAXIS: THE 2.1 ANGSTROM STRUCTURE OF A THREONINE TO ISOLEUCINE MUTANT AT POSITION 87 OF CHEY
Keywords keywordsCHEY, RESPONSE REGULATORS, TWO-COMPONENT SYSTEMS, SIGNAL TRANSDUCTION PROTEIN; SIGNAL TRANSDUCTION PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.76
Radius of gyration Rg (electron density) rg_electron19.79
Forward intensity I(0) i012267200.00
Molecular weight molecular_weight27043.0 kDa
Excluded volume excluded_volume34224 ų
Envelope volume envelope_volume40582 ų
Hydration-shell volume shell_volume17707 ų
Envelope diameter envelope_diameter66.9
Shell Rg shell_rg25.26
Envelope Rg envelope_rg19.78
Shape Rg shape_rg19.81
Total Rg total_rg20.55
Total atoms total_atoms1898
Residues n_residues255
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 dmax68.2
Rg (real space) rg_real20.76
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.2270e+07
I(0) uncertainty (real space) i0_real_error1.6090e+05
Rg (reciprocal space) rg_reciprocal20.76
I(0) (reciprocal space) i0_reciprocal12270000.0000
Solution quality estimate total_estimate0.8037
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3191000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1vlza_
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_idd1vlzb_
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_id1vlzA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1vlzB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator

8. Citations (3)

9. Files and Curves (10)