4xiv

Kinase and Dimerization (P3P4) of the Thermotoga maritima CheA kinase

Method: X-RAY DIFFRACTION
▼

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

Chemotaxis protein CheA

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

UniProt Q56310

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 ADENOSINE-5'-DIPHOSPHATE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CHEA_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–252; UniProt 289–540 Author chain B; PDBConstruct 1–252; UniProt 289–540

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id4xiv
Deposition date deposition_date2015-01-07
Structure title titleKinase and Dimerization (P3P4) of the Thermotoga maritima CheA kinase
Keywords keywordsP3P4, dimerization domain, kinase domain, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4xiv__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4xiv__assembly_1__model_1 | I(q)

10-2 10-1 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

4xiv__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)34.64 Å
Rg (electron density)34.52 Å
Total Rg34.63 Å
Atom count4030
Residues502
Excluded volume72414 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4xiv__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4xiva1
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.2 — Homodimeric domain of signal transducing histidine kinase
Family Family familya.30.2.0 — automated matches
Domain ID domain_idd4xiva2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamilyd.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family familyd.122.1.3 — Histidine kinase
Domain ID domain_idd4xivb1
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.2 — Homodimeric domain of signal transducing histidine kinase
Family Family familya.30.2.0 — automated matches
Domain ID domain_idd4xivb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.122 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Superfamily Superfamily superfamilyd.122.1 — ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase
Family Family familyd.122.1.3 — Histidine kinase
▶

7. Citations (1)