1qfk

STRUCTURE OF HUMAN FACTOR VIIA AND ITS IMPLICATIONS FOR THE TRIGGERING OF BLOOD COAGULATION

Method: X-RAY DIFFRACTION Dmax: 88.2 Å Quality: GOOD

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

COAGULATION FACTOR VIIA 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 Other combination Homooligomer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 213–466 Chain L; UniProt 109–212 Fragment:UNP residues 109-212 Fragment:UNP residues 213-466 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GLC alpha-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 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;50MM NACL, 10MM CACL2, 3.5-3.7M SODIUM FORMATE IN 100MM TRIS PH 8.5, pH 8.50 Resolution 2.80 Å R-free 0.267

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 1–104; UniProt 109–212 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 1qfk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qfk
Deposition date deposition_date1999-04-12
Structure title titleSTRUCTURE OF HUMAN FACTOR VIIA AND ITS IMPLICATIONS FOR THE TRIGGERING OF BLOOD COAGULATION
Keywords keywordsBLOOD COAGULATION, SERINE PROTEASE, 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_guinier24.06
Radius of gyration Rg (electron density) rg_electron23.72
Forward intensity I(0) i051222200.00
Molecular weight molecular_weight36651.0 kDa
Excluded volume excluded_volume35058 ų
Envelope volume envelope_volume59985 ų
Hydration-shell volume shell_volume22697 ų
Envelope diameter envelope_diameter92.0
Shell Rg shell_rg28.41
Envelope Rg envelope_rg24.78
Shape Rg shape_rg23.61
Total Rg total_rg24.28
Total atoms total_atoms2752
Residues n_residues348
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 dmax88.2
Rg (real space) rg_real24.39
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real5.1220e+07
I(0) uncertainty (real space) i0_real_error7.5590e+05
Rg (reciprocal space) rg_reciprocal24.31
I(0) (reciprocal space) i0_reciprocal51220000.0000
Solution quality estimate total_estimate0.7848
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.759
Kurtosis Kurtosis kurtosis0.311
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5970000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.519; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.676; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1qfkh_
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_idd1qfkl1
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_idd1qfkl2
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 (4 domains)

Domain ID domain_id1qfkH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1qfkH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1qfkL01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id1qfkL02
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)