1kli

Cofactor-and substrate-assisted activation of factor VIIa

Method: X-RAY DIFFRACTION Dmax: 67.7 Å Quality: GOOD

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

factor VIIa

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 144–212 Fragment:light chain Fragment:heavy chain SO4 SULFATE ION × 4 CA CALCIUM ION × 1 BEN BENZAMIDINE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;275 K;Ammonium sulphate, glycerol, PEG 400, BICINE, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 275K Resolution 1.69 Å R-free 0.225
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 213–466 Chain L; UniProt 144–212 Fragment:light chain Fragment:heavy chain SO4 SULFATE ION × 8 CA CALCIUM ION × 2 BEN BENZAMIDINE × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;275 K;Ammonium sulphate, glycerol, PEG 400, BICINE, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 275K Resolution 1.69 Å R-free 0.225

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 122 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 1–69; UniProt 144–212 Author chain H; PDBConstruct 1–254; UniProt 213–466

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 1kli

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kli
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kli
Deposition date deposition_date2001-12-12
Structure title titleCofactor-and substrate-assisted activation of factor VIIa
Keywords keywordsextrinsic coagulation pathway, serine protease activation, rational drug design, substrate-assisted catalysis, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.48
Radius of gyration Rg (electron density) rg_electron19.22
Forward intensity I(0) i023284700.00
Molecular weight molecular_weight35449.0 kDa
Excluded volume excluded_volume43818 ų
Envelope volume envelope_volume50791 ų
Hydration-shell volume shell_volume21651 ų
Envelope diameter envelope_diameter68.0
Shell Rg shell_rg26.24
Envelope Rg envelope_rg19.72
Shape Rg shape_rg19.20
Total Rg total_rg20.22
Total atoms total_atoms2477
Residues n_residues292
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 dmax67.7
Rg (real space) rg_real20.37
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.3280e+07
I(0) uncertainty (real space) i0_real_error2.6800e+05
Rg (reciprocal space) rg_reciprocal20.39
I(0) (reciprocal space) i0_reciprocal23290000.0000
Solution quality estimate total_estimate0.8868
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.152
Kurtosis Kurtosis kurtosis-0.443
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha5996000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

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_idd1klih_
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_idd1klil_
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_id1kliH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1kliH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1kliL00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)