2fmf

Crystal structure of CheY in complex with CheZ 200-214 solved from a F432 crystal grown in Hepes (pH 7.5)

Method: X-RAY DIFFRACTION Dmax: 49.9 Å Quality: GOOD

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

Chemotaxis protein cheY

Salmonella typhimurium

UniProt P0A2D5

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 C-terminal 15-mer from Chemotaxis protein cheZ × 1 (P07800) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;2M ammonium sulfate, 0.2M lithium sulfate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.00 Å R-free 0.213

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.

14 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHEY_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–129; UniProt 1–128

C-terminal 15-mer from Chemotaxis protein cheZ

OrganismNot specified

UniProt P07800

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 B; UniProt 200–214 Fragment:residues 200-214 Chemotaxis protein cheY × 1 (P0A2D5) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;2M ammonium sulfate, 0.2M lithium sulfate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.00 Å R-free 0.213

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.

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHEZ_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 200–214

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 2fmf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2fmf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2fmf
Deposition date deposition_date2006-01-09
Structure title titleCrystal structure of CheY in complex with CheZ 200-214 solved from a F432 crystal grown in Hepes (pH 7.5)
Keywords keywordsCHEMOTAXIS; BEF(3)(-)-BOUND CHEY; CHEY-CHEZ PEPTIDE COMPLEX, 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_guinier15.84
Radius of gyration Rg (electron density) rg_electron14.15
Forward intensity I(0) i04710050.00
Molecular weight molecular_weight15547.0 kDa
Excluded volume excluded_volume19549 ų
Envelope volume envelope_volume22121 ų
Hydration-shell volume shell_volume13104 ų
Envelope diameter envelope_diameter49.2
Shell Rg shell_rg20.15
Envelope Rg envelope_rg14.55
Shape Rg shape_rg14.14
Total Rg total_rg15.43
Total atoms total_atoms1089
Residues n_residues141
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 dmax49.9
Rg (real space) rg_real15.72
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real4.7100e+06
I(0) uncertainty (real space) i0_real_error5.8320e+04
Rg (reciprocal space) rg_reciprocal15.73
I(0) (reciprocal space) i0_reciprocal4710000.0000
Solution quality estimate total_estimate0.8858
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha820400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2fmfa_
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_id2fmfA00
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)