12jv

Structural determination of lipid-bound Factor VIII

Method: ELECTRON MICROSCOPY Dmax: 120.2 Å Quality: GOOD

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

Coagulation factor VIII

Homo sapiens

UniProt P00451

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 20–2351 Not recorded 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CALCIUM ION × 1 COPPER (II) ION × 2 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.56 Å

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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2332; UniProt 20–2351

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 12jv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 12jv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id12jv
Deposition date deposition_date2026-04-08
Structure title titleStructural determination of lipid-bound Factor VIII
Keywords keywordsCoagulation, Intrinsic Pathway, Hemophilia, Factor VIII, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.18
Radius of gyration Rg (electron density) rg_electron35.86
Forward intensity I(0) i0306598000.00
Molecular weight molecular_weight143890.0 kDa
Excluded volume excluded_volume180790 ų
Envelope volume envelope_volume235400 ų
Hydration-shell volume shell_volume54441 ų
Envelope diameter envelope_diameter132.7
Shell Rg shell_rg42.10
Envelope Rg envelope_rg36.42
Shape Rg shape_rg35.88
Total Rg total_rg36.24
Total atoms total_atoms10145
Residues n_residues1247
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 dmax120.2
Rg (real space) rg_real36.27
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real3.0660e+08
I(0) uncertainty (real space) i0_real_error5.6460e+06
Rg (reciprocal space) rg_reciprocal36.21
I(0) (reciprocal space) i0_reciprocal306600000.0000
Solution quality estimate total_estimate0.8576
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis-0.049
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85900000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.688

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)