6mf0

Crystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII

Method: X-RAY DIFFRACTION Dmax: 195.6 Å Quality: GOOD

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

Coagulation factor VIII chimera

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 Homooligomer Protein × 2 其他Polymer 6 PDB declaration: monomeric(1) Count mismatch; review required Chain A; UniProt 387–761 Chain A; UniProt 2039–2351 Chain B; UniProt 387–761 Chain B; UniProt 2039–2351 Fragment:UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CA CALCIUM ION × 2 ZN ZINC ION × 2 CU1 COPPER (I) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;16% PEG3350, 0.025 M magnesium chloride, 0.025 M HEPES Resolution 3.20 Å R-free 0.287
2 Insufficient information Monomer Protein × 1 其他Polymer 3 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 387–761 Chain A; UniProt 2039–2351 Fragment:UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;16% PEG3350, 0.025 M magnesium chloride, 0.025 M HEPES Resolution 3.20 Å R-free 0.287

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

Coagulation factor VIII chimera

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 Homooligomer Protein × 2 其他Polymer 6 PDB declaration: monomeric(1) Count mismatch; review required Chain A; UniProt 1–386 Chain A; UniProt 762–771 Chain A; UniProt 1438–1820 Chain B; UniProt 1–386 Chain B; UniProt 762–771 Chain B; UniProt 1438–1820 Fragment:UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CA CALCIUM ION × 2 ZN ZINC ION × 2 CU1 COPPER (I) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;16% PEG3350, 0.025 M magnesium chloride, 0.025 M HEPES Resolution 3.20 Å R-free 0.287
2 Insufficient information Monomer Protein × 1 其他Polymer 3 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–386 Chain A; UniProt 762–771 Chain A; UniProt 1438–1820 Fragment:UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1 CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;16% PEG3350, 0.025 M magnesium chloride, 0.025 M HEPES Resolution 3.20 Å R-free 0.287

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 6 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 Author chain B; PDBConstruct 1–386; UniProt 1–386 Author chain B; PDBConstruct 762–771; UniProt 762–771 Author chain B; 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 6mf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mf0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mf0
Deposition date deposition_date2018-09-07
Structure title titleCrystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII
Keywords keywordsHemostasis, Hemophilia A, Factor VIII, Chimera, 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_guinier55.64
Radius of gyration Rg (electron density) rg_electron56.05
Forward intensity I(0) i01193170000.00
Molecular weight molecular_weight292470.0 kDa
Excluded volume excluded_volume367120 ų
Envelope volume envelope_volume498990 ų
Hydration-shell volume shell_volume77773 ų
Envelope diameter envelope_diameter219.8
Shell Rg shell_rg53.23
Envelope Rg envelope_rg56.27
Shape Rg shape_rg56.04
Total Rg total_rg56.00
Total atoms total_atoms20616
Residues n_residues2503
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 dmax195.6
Rg (real space) rg_real56.15
Rg uncertainty (real space) rg_real_error2.83
I(0) (real space) i0_real1.1930e+09
I(0) uncertainty (real space) i0_real_error2.8550e+07
Rg (reciprocal space) rg_reciprocal55.20
I(0) (reciprocal space) i0_reciprocal1191000000.0000
Solution quality estimate total_estimate0.7564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.9
Skewness Skewness skewness0.544
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha140700000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.807; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6mf0A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id6mf0B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like

8. Citations (3)

9. Files and Curves (10)