2ceh

Phosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TISSUE FACTOR

OrganismNot specified

UniProt P13726

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TF_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–19; UniProt 277–295

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ceh
Deposition date deposition_date2006-02-06
Structure title titlePhosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity
Keywords keywords;UNPHOSPHORYLATED, PIN1, WW DOMAIN, BLOOD COAGULATION, GLYCOPROTEIN, LIPOPROTEIN, PALMITATE, POLYMORPHISM, TRANSMEMBRANE, COAGULATION PROTEIN, BLOOD CLOTTING ;; BLOOD CLOTTING
Experimental Method methodSOLUTION NMR
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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.

2ceh__assembly_1__model_7

Assembly 1 · Model 7 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2ceh__assembly_1__model_7 | I(q)

10-2 10-1 104 105 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

2ceh__assembly_1__model_7 | 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)10.76 Å
Rg (electron density)9.57 Å
Total Rg11.12 Å
Atom count262
Residues19
Excluded volume2517 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2ceh__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2ceh__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2ceh__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2ceh__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2ceh__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2ceh__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2ceh__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2ceh__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2ceh__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2ceh__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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7. Citations (1)