2ceh

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

Method: SOLUTION NMR Dmax: 43.9 Å Quality: GOOD

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

TISSUE FACTOR

OrganismNot specified

UniProt P13726

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 277–295 Fragment:TISSUE FACTOR CYTOPLASMIC DOMAIN, RESIDUES 277-295 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;285 K;Ionic strength (raw mmCIF value) 0;Pressure 1.0 NMR measurement conditions:pH 6;285 K;Ionic strength (raw mmCIF value) 0;Pressure 1.0 NMR sample composition:90% WATER 10% D2O Resolution not provided

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.

52 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 2ceh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ceh
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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

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

Radius of gyration Rg (Guinier) rg_guinier10.74
Radius of gyration Rg (electron density) rg_electron10.08
Forward intensity I(0) i08234130.00
Molecular weight molecular_weight20623.0 kDa
Excluded volume excluded_volume25166 ų
Envelope volume envelope_volume10767 ų
Hydration-shell volume shell_volume7961 ų
Envelope diameter envelope_diameter44.4
Shell Rg shell_rg17.17
Envelope Rg envelope_rg12.81
Shape Rg shape_rg9.95
Total Rg total_rg11.27
Total atoms total_atoms2620
Residues n_residues190
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 dmax43.9
Rg (real space) rg_real10.87
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.2340e+06
I(0) uncertainty (real space) i0_real_error9.5260e+04
Rg (reciprocal space) rg_reciprocal10.87
I(0) (reciprocal space) i0_reciprocal8234000.0000
Solution quality estimate total_estimate0.7572
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.8
Skewness Skewness skewness0.543
Kurtosis Kurtosis kurtosis0.065
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12050.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.546; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.219; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)