3hob

Factor VIII Trp2313-His2315 segment is involved in membrane binding as shown by crystal structure of complex between factor VIII C2 domain and an inhibitor

Method: X-RAY DIFFRACTION Dmax: 71.5 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 M; UniProt 2189–2347 Fragment:factor VIII c2 domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;30.0% PEG 2000, MME 0.15M KBr, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.07 Å R-free 0.263
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2189–2347 Fragment:factor VIII c2 domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;30.0% PEG 2000, MME 0.15M KBr, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.07 Å R-free 0.263

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 1–159; UniProt 2189–2347 Author chain M; PDBConstruct 1–159; UniProt 2189–2347

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 3hob

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hob
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3hob
Deposition date deposition_date2009-06-01
Structure title titleFactor VIII Trp2313-His2315 segment is involved in membrane binding as shown by crystal structure of complex between factor VIII C2 domain and an inhibitor
Keywords keywords;BLOOD CLOTTING, Acute phase, Blood coagulation, Calcium, Disease mutation, Disulfide bond, Glycoprotein, Hemophilia, Metal-binding, Pharmaceutical, Polymorphism, Secreted, Sulfation ;; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.18
Radius of gyration Rg (electron density) rg_electron21.57
Forward intensity I(0) i021214800.00
Molecular weight molecular_weight35313.0 kDa
Excluded volume excluded_volume44266 ų
Envelope volume envelope_volume51552 ų
Hydration-shell volume shell_volume20338 ų
Envelope diameter envelope_diameter73.1
Shell Rg shell_rg27.57
Envelope Rg envelope_rg21.66
Shape Rg shape_rg21.52
Total Rg total_rg22.48
Total atoms total_atoms2484
Residues n_residues312
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 dmax71.5
Rg (real space) rg_real22.18
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real2.1210e+07
I(0) uncertainty (real space) i0_real_error2.9530e+05
Rg (reciprocal space) rg_reciprocal22.18
I(0) (reciprocal space) i0_reciprocal21210000.0000
Solution quality estimate total_estimate0.8941
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.557
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5285000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3hoba_
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.2 — Discoidin domain (FA58C, coagulation factor 5/8 C-terminal domain)
Domain ID domain_idd3hobm_
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.2 — Discoidin domain (FA58C, coagulation factor 5/8 C-terminal domain)

CATH v4.4 (2 domains)

Domain ID domain_id3hobA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id3hobM00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like

8. Citations (1)

9. Files and Curves (10)