2r7e

Crystal Structure Analysis of Coagulation Factor VIII

Method: X-RAY DIFFRACTION Dmax: 125.7 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 Other combination Homooligomer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–760 Chain B; UniProt 1582–2351 Fragment:residues 19-760 Fragment:residues 1582-2351 Mutation:F1838S ;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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-2)-beta-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)-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 × 3 CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;8-10% PEG 8000, 0.1M Imidazole, 100-300 mM NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.70 Å R-free 0.347

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–742; UniProt 19–760 Author chain B; PDBConstruct 1–770; UniProt 1582–2351

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 2r7e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2r7e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2r7e
Deposition date deposition_date2007-09-07
Structure title titleCrystal Structure Analysis of Coagulation Factor VIII
Keywords keywords;ceruloplasmin fold, cupper protein fold, C2 domain fold, Acute phase, Blood coagulation, Disease mutation, Glycoprotein, Hemophilia, Metal-binding, Secreted, Sulfation, 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_guinier37.50
Radius of gyration Rg (electron density) rg_electron37.06
Forward intensity I(0) i0363887000.00
Molecular weight molecular_weight155930.0 kDa
Excluded volume excluded_volume195480 ų
Envelope volume envelope_volume267830 ų
Hydration-shell volume shell_volume59429 ų
Envelope diameter envelope_diameter133.3
Shell Rg shell_rg43.58
Envelope Rg envelope_rg37.35
Shape Rg shape_rg37.08
Total Rg total_rg37.42
Total atoms total_atoms10985
Residues n_residues1337
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 dmax125.7
Rg (real space) rg_real37.52
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real3.6390e+08
I(0) uncertainty (real space) i0_real_error6.6510e+06
Rg (reciprocal space) rg_reciprocal37.51
I(0) (reciprocal space) i0_reciprocal363900000.0000
Solution quality estimate total_estimate0.8683
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.9
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.164
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72840000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id2r7eA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eA04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2r7eB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id2r7eB04
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)