4zma

Crystal Structure of a FVIIa-Trypsin Chimera (ST) in Complex with Soluble Tissue Factor

Method: X-RAY DIFFRACTION Dmax: 111.3 Å Quality: GOOD

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

Coagulation factor VII

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 61–212 Non-standard monomer:Yes (specific site not provided by mmCIF) Fragment:UNP residues 213-466 Mutation:169-175 LQQSRKVGDSPN -> EASSPGK Tissue factor × 1 (P13726) CA CALCIUM ION × 8 BGC beta-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 0Z6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide × 1 CAC CACODYLATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.1;295 K;0.1M Cacodylate,11% PEG 8000 , with seeding Resolution 2.30 Å R-free 0.295

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 1–152; UniProt 61–212 Author chain H; PDBConstruct 1–249; 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 33–251 Not recorded Coagulation factor VII × 1 (P08709) Coagulation factor VII × 1 (P08709) CA CALCIUM ION × 8 BGC beta-D-glucopyranose × 1 FUC alpha-L-fucopyranose × 1 0Z6 D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide × 1 CAC CACODYLATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.1;295 K;0.1M Cacodylate,11% PEG 8000 , with seeding Resolution 2.30 Å R-free 0.295

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 1–219; 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 4zma

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4zma
Deposition date deposition_date2015-05-02
Structure title titleCrystal Structure of a FVIIa-Trypsin Chimera (ST) in Complex with Soluble Tissue Factor
Keywords keywordsfusion protein, trypsin-fold, protein-protein complex, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.46
Radius of gyration Rg (electron density) rg_electron32.62
Forward intensity I(0) i073285900.00
Molecular weight molecular_weight65776.0 kDa
Excluded volume excluded_volume81060 ų
Envelope volume envelope_volume103770 ų
Hydration-shell volume shell_volume28963 ų
Envelope diameter envelope_diameter119.5
Shell Rg shell_rg35.83
Envelope Rg envelope_rg32.93
Shape Rg shape_rg32.47
Total Rg total_rg33.35
Total atoms total_atoms8881
Residues n_residues567
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 dmax111.3
Rg (real space) rg_real32.99
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real7.3290e+07
I(0) uncertainty (real space) i0_real_error1.3580e+06
Rg (reciprocal space) rg_reciprocal32.77
I(0) (reciprocal space) i0_reciprocal73270000.0000
Solution quality estimate total_estimate0.7860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.616
Kurtosis Kurtosis kurtosis-0.300
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9405000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.640; Smooth: 0.626

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd4zmah_
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_idd4zmal1
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_idd4zmal2
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_idd4zmal3
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_idd4zmat1
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_idd4zmat2
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_id4zmaH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4zmaH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4zmaT01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4zmaT02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)