9d5d

Crystal Structure of Blood Coagulation Factor VIII C2 Domain Mutant L2251A/L2252A

Method: X-RAY DIFFRACTION Dmax: 56.1 Å Quality: GOOD

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

Factor VIIIa light chain

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 M; UniProt 2191–2351 Fragment:C2 domain (UNP residues 2191-2351) Mutation:L2251A,L2252A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;4 M potassium formate, 0.1 M Bis-Tris propane, pH 9, 2% w/v PEG2000 MME Resolution 1.83 Å R-free 0.223

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 M; PDBConstruct 4–164; UniProt 2191–2351

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 9d5d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d5d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d5d
Deposition date deposition_date2024-08-13
Structure title titleCrystal Structure of Blood Coagulation Factor VIII C2 Domain Mutant L2251A/L2252A
Keywords keywordsBlood coagulation factor VIII, lipid binding protein, factor VIII C2 domain mutant, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.14
Radius of gyration Rg (electron density) rg_electron14.90
Forward intensity I(0) i06151310.00
Molecular weight molecular_weight17814.0 kDa
Excluded volume excluded_volume22239 ų
Envelope volume envelope_volume24555 ų
Hydration-shell volume shell_volume13878 ų
Envelope diameter envelope_diameter55.4
Shell Rg shell_rg20.94
Envelope Rg envelope_rg15.34
Shape Rg shape_rg14.86
Total Rg total_rg16.13
Total atoms total_atoms1253
Residues n_residues158
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 dmax56.1
Rg (real space) rg_real16.04
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real6.1510e+06
I(0) uncertainty (real space) i0_real_error8.1100e+04
Rg (reciprocal space) rg_reciprocal16.05
I(0) (reciprocal space) i0_reciprocal6151000.0000
Solution quality estimate total_estimate0.8539
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.201
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1305000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.704; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)