7kbt

Factor VIII in complex with the anti-C2 domain antibody, G99

Method: X-RAY DIFFRACTION Dmax: 147.6 Å Quality: GOOD

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

Coagulation factor VIII,Coagulation factor VIII,Coagulation factor VIII,Coagulation factor VIII,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 Insufficient information Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 387–761 Chain A; UniProt 2039–2351 Not recorded G99 heavy chain × 1 G99 light chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;8 - 18% PEG 1500, PEG 6K, or PEG 10K and 50mM malic acid, pH 7. Resolution 4.15 Å R-free 0.338

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 387–761; UniProt 387–761 Author chain A; PDBConstruct 1155–1467; UniProt 2039–2351

Coagulation factor VIII,Coagulation factor VIII,Coagulation factor VIII,Coagulation factor VIII,Coagulation factor VIII

Homo sapiens

UniProt P12263

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 其他Polymer 2 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–386 Chain A; UniProt 762–771 Chain A; UniProt 1438–1820 Not recorded G99 heavy chain × 1 G99 light chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;8 - 18% PEG 1500, PEG 6K, or PEG 10K and 50mM malic acid, pH 7. Resolution 4.15 Å R-free 0.338

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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA8_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–386; UniProt 1–386 Author chain A; PDBConstruct 762–771; UniProt 762–771 Author chain A; PDBConstruct 772–1154; UniProt 1438–1820

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 7kbt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kbt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kbt
Deposition date deposition_date2020-10-02
Structure title titleFactor VIII in complex with the anti-C2 domain antibody, G99
Keywords keywordsAntibody, inhibitor, BLOOD CLOTTING, BLOOD CLOTTING-Immune System complex; BLOOD CLOTTING/Immune System
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.88
Radius of gyration Rg (electron density) rg_electron41.56
Forward intensity I(0) i0397422000.00
Molecular weight molecular_weight161270.0 kDa
Excluded volume excluded_volume200920 ų
Envelope volume envelope_volume279480 ų
Hydration-shell volume shell_volume57723 ų
Envelope diameter envelope_diameter149.0
Shell Rg shell_rg44.88
Envelope Rg envelope_rg42.32
Shape Rg shape_rg41.57
Total Rg total_rg41.70
Total atoms total_atoms11366
Residues n_residues1444
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 dmax147.6
Rg (real space) rg_real42.12
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real3.9740e+08
I(0) uncertainty (real space) i0_real_error7.5120e+06
Rg (reciprocal space) rg_reciprocal41.88
I(0) (reciprocal space) i0_reciprocal397300000.0000
Solution quality estimate total_estimate0.8429
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.7
Skewness Skewness skewness0.531
Kurtosis Kurtosis kurtosis-0.247
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha70720000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)