1boy

EXTRACELLULAR REGION OF HUMAN TISSUE FACTOR

Method: X-RAY DIFFRACTION Dmax: 87.3 Å Quality: REASONABLE

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

HUMAN TISSUE FACTOR

Homo sapiens

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 33–251 Fragment:EXTRACELLULAR DOMAIN, RESIDUES 1 - 219 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å

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 1–219; UniProt 33–251

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 1boy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1boy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1boy
Deposition date deposition_date1996-01-11
Structure title titleEXTRACELLULAR REGION OF HUMAN TISSUE FACTOR
Keywords keywordsINITIATOR OF BLOOD COAGULATION IN VERTEBRATES, COFACTOR FOR FACTOR VIIA, CLASS 2 CYTOKINE RECEPTOR, GLYCOPROTEIN, BLOOD COAGULATION; CLASS 2 CYTOKINE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.63
Radius of gyration Rg (electron density) rg_electron23.17
Forward intensity I(0) i010377700.00
Molecular weight molecular_weight23890.0 kDa
Excluded volume excluded_volume29815 ų
Envelope volume envelope_volume36858 ų
Hydration-shell volume shell_volume15031 ų
Envelope diameter envelope_diameter89.6
Shell Rg shell_rg27.07
Envelope Rg envelope_rg23.76
Shape Rg shape_rg23.15
Total Rg total_rg23.80
Total atoms total_atoms1684
Residues n_residues211
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 dmax87.3
Rg (real space) rg_real24.02
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.0380e+07
I(0) uncertainty (real space) i0_real_error1.6050e+05
Rg (reciprocal space) rg_reciprocal23.93
I(0) (reciprocal space) i0_reciprocal10380000.0000
Solution quality estimate total_estimate0.7407
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.648
Kurtosis Kurtosis kurtosis-0.125
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3976000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.470; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.223; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1boya1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III
Domain ID domain_idd1boya2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.2 — Fibronectin type III
Family Family familyb.1.2.1 — Fibronectin type III

CATH v4.4 (2 domains)

Domain ID domain_id1boyA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1boyA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)