4m7l

Crystal structure of the complex between human tissue factor extracellular domain and antibody 10H10 FAB fragment

Method: X-RAY DIFFRACTION Dmax: 105.7 Å Quality: GOOD

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

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain T; UniProt 37–245 Fragment:extracellular domain (UNP residues 37-245) 10H10 light chain × 1 10H10 heavy chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 10.5;293 K;0.1 M CAPS, pH 10.5, 24% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.40 Å R-free 0.289

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 T; PDBConstruct 1–209; UniProt 37–245

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 4m7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4m7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4m7l
Deposition date deposition_date2013-08-12
Structure title titleCrystal structure of the complex between human tissue factor extracellular domain and antibody 10H10 FAB fragment
Keywords keywordsantibody, BLOOD CLOTTING-IMMUNE SYSTEM complex; BLOOD CLOTTING/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.40
Radius of gyration Rg (electron density) rg_electron31.23
Forward intensity I(0) i078130400.00
Molecular weight molecular_weight69835.0 kDa
Excluded volume excluded_volume87219 ų
Envelope volume envelope_volume111490 ų
Hydration-shell volume shell_volume31869 ų
Envelope diameter envelope_diameter112.1
Shell Rg shell_rg35.89
Envelope Rg envelope_rg31.31
Shape Rg shape_rg31.18
Total Rg total_rg31.76
Total atoms total_atoms4919
Residues n_residues636
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 dmax105.7
Rg (real space) rg_real31.62
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real7.8130e+07
I(0) uncertainty (real space) i0_real_error1.2310e+06
Rg (reciprocal space) rg_reciprocal31.53
I(0) (reciprocal space) i0_reciprocal78120000.0000
Solution quality estimate total_estimate0.8610
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.498
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10620000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.917; Smooth: 0.719

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4m7lH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4m7lH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4m7lL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4m7lL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4m7lT01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4m7lT02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)