1a0o

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY

Method: X-RAY DIFFRACTION Dmax: 171.8 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–128 Not recorded CHEA × 1 (P07363) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–128 Not recorded CHEA × 1 (P07363) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–128 Not recorded CHEA × 1 (P07363) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–128 Not recorded CHEA × 1 (P07363) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235

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 43 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 C; PDBConstruct 1–128; UniProt 1–128 Author chain E; PDBConstruct 1–128; UniProt 1–128 Author chain G; PDBConstruct 1–128; UniProt 1–128

CHEA

Escherichia coli

UniProt P07363

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 124–257 Fragment:CHEA 124-257 CHEY × 1 (P06143) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 124–257 Fragment:CHEA 124-257 CHEY × 1 (P06143) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 124–257 Fragment:CHEA 124-257 CHEY × 1 (P06143) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 124–257 Fragment:CHEA 124-257 CHEY × 1 (P06143) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE Resolution 2.95 Å R-free 0.235

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHEA_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–134; UniProt 124–257 Author chain D; PDBConstruct 1–134; UniProt 124–257 Author chain F; PDBConstruct 1–134; UniProt 124–257 Author chain H; PDBConstruct 1–134; UniProt 124–257

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 1a0o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a0o
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1a0o
Deposition date deposition_date1997-12-05
Structure title titleCHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY
Keywords keywordsBACTERIAL CHEMOTAXIS, SIGNAL TRANSDUCTION, TWO-COMPONENT SYSTEM, HISTIDINE KINASE, RESPONSE REGULATOR, CHEMOTAXIS; CHEMOTAXIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.82
Radius of gyration Rg (electron density) rg_electron56.93
Forward intensity I(0) i0100824000.00
Molecular weight molecular_weight85206.0 kDa
Excluded volume excluded_volume107470 ų
Envelope volume envelope_volume183830 ų
Hydration-shell volume shell_volume28672 ų
Envelope diameter envelope_diameter180.2
Shell Rg shell_rg56.13
Envelope Rg envelope_rg52.65
Shape Rg shape_rg56.91
Total Rg total_rg56.97
Total atoms total_atoms5969
Residues n_residues785
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 dmax171.8
Rg (real space) rg_real57.08
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real1.0080e+08
I(0) uncertainty (real space) i0_real_error2.0000e+06
Rg (reciprocal space) rg_reciprocal56.56
I(0) (reciprocal space) i0_reciprocal100700000.0000
Solution quality estimate total_estimate0.6218
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.6
Skewness Skewness skewness0.147
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2396000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.085; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.738; Smooth: 0.087

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1a0oa_
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_idd1a0ob_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.24 — CheY-binding domain of CheA
Family Family familyd.58.24.1 — CheY-binding domain of CheA
Domain ID domain_idd1a0oc_
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_idd1a0od_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.24 — CheY-binding domain of CheA
Family Family familyd.58.24.1 — CheY-binding domain of CheA
Domain ID domain_idd1a0oe_
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_idd1a0of_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.24 — CheY-binding domain of CheA
Family Family familyd.58.24.1 — CheY-binding domain of CheA
Domain ID domain_idd1a0og_
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_idd1a0oh_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.24 — CheY-binding domain of CheA
Family Family familyd.58.24.1 — CheY-binding domain of CheA

CATH v4.4 (8 domains)

Domain ID domain_id1a0oA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1a0oB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily400 — CheY-binding domain of CheA
Domain ID domain_id1a0oC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1a0oD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily400 — CheY-binding domain of CheA
Domain ID domain_id1a0oE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1a0oF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily400 — CheY-binding domain of CheA
Domain ID domain_id1a0oG00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2300 — Response regulator
Domain ID domain_id1a0oH00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily400 — CheY-binding domain of CheA

8. Citations (1)

9. Files and Curves (10)