2b8o

Crystal Structure of Glu-Gly-Arg-Chloromethyl Ketone-Factor VIIa/Soluble Tissue Factor Complex

Method: X-RAY DIFFRACTION Dmax: 116.1 Å Quality: GOOD

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

Coagulation factor VII light chain

Homo sapiens

UniProt P08709

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 H; UniProt 213–466 Chain L; UniProt 61–202 Non-standard monomer:Yes (specific site not provided by mmCIF) Tissue factor × 1 (P13726) GLC alpha-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 CA CALCIUM ION × 6 MG MAGNESIUM ION × 2 0GJ L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide × 1 NA SODIUM ION × 1 ZN ZINC ION × 2 CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;Tris, sodium chloride, calcium chloride, PEG 4000, ADA, magnesium chloride, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.80 Å R-free 0.285

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.

113 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA7_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain L; PDBConstruct 1–142; UniProt 61–202 Author chain H; PDBConstruct 1–254; UniProt 213–466

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 38–242 Not recorded Coagulation factor VII light chain × 1 (P08709) Coagulation factor VII heavy chain × 1 (P08709) GLC alpha-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 CA CALCIUM ION × 6 MG MAGNESIUM ION × 2 0GJ L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide × 1 NA SODIUM ION × 1 ZN ZINC ION × 2 CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;298 K;Tris, sodium chloride, calcium chloride, PEG 4000, ADA, magnesium chloride, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.80 Å R-free 0.285

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 3
Chains and sequence ranges Author chain T; PDBConstruct 1–205; UniProt 38–242

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 2b8o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b8o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b8o
Deposition date deposition_date2005-10-08
Structure title titleCrystal Structure of Glu-Gly-Arg-Chloromethyl Ketone-Factor VIIa/Soluble Tissue Factor Complex
Keywords keywords;Serine protease, Tissue factor, EGR, blood coagualtion, clotting, clotting factor, coagulation factor, hydrolase-hydrolase inhibitor COMPLEX ;; hydrolase/hydrolase inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.51
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i0143151000.00
Molecular weight molecular_weight63024.0 kDa
Excluded volume excluded_volume60432 ų
Envelope volume envelope_volume108020 ų
Hydration-shell volume shell_volume29880 ų
Envelope diameter envelope_diameter122.6
Shell Rg shell_rg36.07
Envelope Rg envelope_rg33.23
Shape Rg shape_rg32.74
Total Rg total_rg33.18
Total atoms total_atoms4720
Residues n_residues554
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 dmax116.1
Rg (real space) rg_real33.06
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real1.4320e+08
I(0) uncertainty (real space) i0_real_error2.6030e+06
Rg (reciprocal space) rg_reciprocal32.83
I(0) (reciprocal space) i0_reciprocal143100000.0000
Solution quality estimate total_estimate0.7789
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.647
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12500000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.581; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.539; Smooth: 0.841

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2b8oh_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd2b8ol1
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module
Domain ID domain_idd2b8ol2
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module
Domain ID domain_idd2b8ol3
Class classg — Small proteins
Fold Fold foldg.32 — GLA-domain
Superfamily Superfamily superfamilyg.32.1 — GLA-domain
Family Family familyg.32.1.1 — GLA-domain
Domain ID domain_idd2b8ot1
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_idd2b8ot2
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 (4 domains)

Domain ID domain_id2b8oH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2b8oH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id2b8oT01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2b8oT02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)