SAXSdb — 4mo3

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

Coagulation factor VIII

Sus scrofa

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 1971–2129	Fragment：C2 domain (UNP residues 1971-2129)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 10.4；277 K；2:1 crystallization buffer (0.1 M magnesium acetate, 10% ethanol) to protein, crystals formed overnight with 0.1 M CHES buffer and 220 uL Hampton Research Al's oil over 400 uL reservoir, pH 10.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.70 Å R-free 0.209

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.

Other PDB	Difference from Current Entry 4MO3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6MF0 Crystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII Deposited 2018-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: monomeric	Chain A 1–386（386 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain A 762–771（10 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain A 1438–1820（383 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain B 1–386（386 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain B 762–771（10 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain B 1438–1820（383 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human)	Not recorded	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
6MF0 Crystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII Deposited 2018-09-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–386（386 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain A 762–771（10 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human) Chain A 1438–1820（383 aa） Fragment：UNP residues 1-386 (pig), 387-761 (human), 762-771,1438-1820 (pig), 2039-2351 (human)	Not recorded	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
7K66 Structure of Blood Coagulation Factor VIII in Complex with an Anti-C1 Domain Pathogenic Antibody Inhibitor Deposited 2020-09-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–405（405 aa） Chain A 1438–1820（383 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CU COPPER (II) ION × 1 CA CALCIUM ION × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.7；293 K；17.5 %(w/v) PEG 1500, 50 mM HEPES (pH 7.7)	Resolution 3.92 Å R-free 0.322
7KBT Factor VIII in complex with the anti-C2 domain antibody, G99 Deposited 2020-10-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–386（386 aa） Chain A 762–771（10 aa） Chain A 1438–1820（383 aa）	Not recorded	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
7S0P Crystal structure of Porcine Factor VIII C2 Domain Bound to Phosphatidylserine Deposited 2021-08-30	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain M 1974–2129（156 aa）	Not recorded	SEP PHOSPHOSERINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2:1 drop ratio 0.1 M CHES (pH 7.4) 0.1M magnesium acetate 10% ethanol (v/v) Crystal soaked with 5 mM OPLS	Resolution 1.30 Å R-free 0.156
8G6I Coagulation factor VIII bound to a patient-derived anti-C1 domain antibody inhibitor Deposited 2023-02-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–405（405 aa） Chain A 1438–1820（383 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；150 mM NaCl, 20 mM HEPES pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.23 Å
8TY1 Cryo-EM structure of coagulation factor VIII bound to NB2E9 Deposited 2023-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–391（391 aa） Chain A 1438–1820（383 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；20 mM HEPES (pH 7.4) and 150 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.46 Å

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 M； PDBConstruct 19–177； UniProt 1971–2129

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4mo3
Deposition date deposition_date	2013-09-11
Structure title title	Crystal Structure of Porcine C2 Domain of Blood Coagulation Factor VIII
Keywords keywords	Blood coagulation domain, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	16.09 Å
Radius of gyration Rg (electron density) rg_electron	14.89 Å
Forward intensity I(0) i0	6057720.00
Molecular weight molecular_weight	17490.0 kDa
Excluded volume excluded_volume	21815 Å³
Envelope volume envelope_volume	24464 Å³
Hydration-shell volume shell_volume	13802 Å³
Envelope diameter envelope_diameter	53.6 Å
Shell Rg shell_rg	20.98 Å
Envelope Rg envelope_rg	15.43 Å
Shape Rg shape_rg	14.85 Å
Total Rg total_rg	16.14 Å
Total atoms total_atoms	1231
Residues n_residues	156
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	56.1 Å
Rg (real space) rg_real	15.99 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	6.0580e+06
I(0) uncertainty (real space) i0_real_error	7.4720e+04
Rg (reciprocal space) rg_reciprocal	16.00 Å
I(0) (reciprocal space) i0_reciprocal	6058000.0000
Solution quality estimate total_estimate	0.8524
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.3 Å
Skewness Skewness skewness	0.166
Kurtosis Kurtosis kurtosis	-0.292
Angular range angular_range	— – 0.4950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1217000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.696; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.997

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Coagulation factor VIII
Molecular weight formula_weight	19903.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M
Atom count atom_count	1442

MGSSHHHHHHENLYFQGSDLNSCSMPLGMQNKAISDSQITASSHLSNIFATWSPSQARLHLQGRTNAWRPRVSSAEEWLQVDLQKTVKVTGITTQGVKSLLSSMYVKEFLVSSSQDGRRWTLFLQDGHTKVFQGNQDSSTPVVNALDPPLFTRYLRIHPTSWAQHIALRLEVLGCEA

来源 Source

来源生物 organism	Sus scrofa
通用名 common_name	pig
NCBI Class编号 ncbi_taxonomy_id	9823
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	179

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d4mo3m_
Class class	b — All beta proteins
Fold Fold fold	b.18 — Galactose-binding domain-like
Superfamily Superfamily superfamily	b.18.1 — Galactose-binding domain-like
Family Family family	b.18.1.2 — Discoidin domain (FA58C, coagulation factor 5/8 C-terminal domain)

CATH v4.4 (1 domains)

Domain ID domain_id	4mo3M00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	260 — Galactose-binding domain-like

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8. Citations (1)

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Unit-cell length a length_a	49.070 Å
Unit-cell length b length_b	68.940 Å
Unit-cell length c length_c	105.960 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	1.702 Å
Low-resolution limit resolution_low	31.912 Å
R factor r_factor	0.1786
R_work r_work	0.1752
R_free r_free	0.2093

fit	/app/data/saxs_computation/mo/4mo3/4mo3.fit
pddf	/app/data/pr_computation/mo/4mo3/4mo3.pr.out
profile	/app/data/saxs_computation/mo/4mo3/4mo3.dat

Crystal Structure of Porcine C2 Domain of Blood Coagulation Factor VIII

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

Coagulation factor VIII

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction