5tqe

Factor VIIa in complex with the inhibitor (5R)-5-[(1-aminoisoquinolin-6-yl)amino]-19-(cyclopropylsulfonyl)-3-methyl-13-oxa-3,15-diazatricyclo[14.3.1.1~6,10~]henicosa-1(20),6(21),7,9,16,18-hexaene-4,14-dione

Method: X-RAY DIFFRACTION Dmax: 64.4 Å Quality: GOOD

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

Factor VIIa (Heavy 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 213–466 Chain L; UniProt 150–204 Not recorded 7KQ (5R)-5-[(1-aminoisoquinolin-6-yl)amino]-19-(cyclopropylsulfonyl)-3-methyl-13-oxa-3,15-diazatricyclo[14.3.1.1~6,10~]henicosa-1(20),6(21),7,9,16,18-hexaene-4,14-dione × 1 CA CALCIUM ION × 1 SO4 SULFATE ION × 4 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;100 mM MES, pH 6.0, 20 mM CACL2, 17.5%(W/V) PEG 6000 Resolution 1.90 Å R-free 0.209

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 H; PDBConstruct 1–254; UniProt 213–466 Author chain L; PDBConstruct 1–55; UniProt 150–204

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 5tqe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5tqe
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5tqe
Deposition date deposition_date2016-10-24
Structure title titleFactor VIIa in complex with the inhibitor (5R)-5-[(1-aminoisoquinolin-6-yl)amino]-19-(cyclopropylsulfonyl)-3-methyl-13-oxa-3,15-diazatricyclo[14.3.1.1~6,10~]henicosa-1(20),6(21),7,9,16,18-hexaene-4,14-dione
Keywords keywords;GLYCOPROTEIN, HYDROLASE, SERINE PROTEASE, PLASMA, BLOOD COAGULATION FACTOR, PROTEIN INHIBITOR COMPLEX, CALCIUM-BINDING, 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_guinier19.97
Radius of gyration Rg (electron density) rg_electron18.69
Forward intensity I(0) i022320900.00
Molecular weight molecular_weight34909.0 kDa
Excluded volume excluded_volume43195 ų
Envelope volume envelope_volume49116 ų
Hydration-shell volume shell_volume21407 ų
Envelope diameter envelope_diameter66.1
Shell Rg shell_rg25.68
Envelope Rg envelope_rg19.12
Shape Rg shape_rg18.67
Total Rg total_rg19.69
Total atoms total_atoms2470
Residues n_residues286
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 dmax64.4
Rg (real space) rg_real19.82
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.2320e+07
I(0) uncertainty (real space) i0_real_error2.5910e+05
Rg (reciprocal space) rg_reciprocal19.84
I(0) (reciprocal space) i0_reciprocal22320000.0000
Solution quality estimate total_estimate0.8908
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.127
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5482000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5tqeh_
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_idd5tqel_
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

CATH v4.4 (3 domains)

Domain ID domain_id5tqeH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id5tqeH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id5tqeL00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)