1u0n

The ternary von Willebrand Factor A1-glycoprotein Ibalpha-botrocetin complex

Method: X-RAY DIFFRACTION Dmax: 91.8 Å Quality: EXCELLENT

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

Von Willebrand factor

Homo sapiens

UniProt P04275

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1261–1468 Fragment:VWFA 1 Botrocetin × 1 (P22029) Botrocetin × 1 (P22030) Platelet glycoprotein Ib × 1 (P07359) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;Sodium citrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.95 Å R-free 0.276

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.

46 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VWF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–208; UniProt 1261–1468

Botrocetin

OrganismNot specified

UniProt P22029

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–133 Fragment:Alpha chain Von Willebrand factor × 1 (P04275) Botrocetin × 1 (P22030) Platelet glycoprotein Ib × 1 (P07359) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;Sodium citrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.95 Å R-free 0.276

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BOTA_BOTJA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–133; UniProt 1–133

Botrocetin

OrganismNot specified

UniProt P22030

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–125 Fragment:Beta chain Von Willebrand factor × 1 (P04275) Botrocetin × 1 (P22029) Platelet glycoprotein Ib × 1 (P07359) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;Sodium citrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.95 Å R-free 0.276

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BOTB_BOTJA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–125; UniProt 1–125

Platelet glycoprotein Ib

Homo sapiens

UniProt P07359

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 17–281 Fragment:Alpha chain Mutation:N21Q,N159Q Von Willebrand factor × 1 (P04275) Botrocetin × 1 (P22029) Botrocetin × 1 (P22030) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;Sodium citrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.95 Å R-free 0.276

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.

20 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP1BA_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–265; UniProt 17–281

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 1u0n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1u0n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1u0n
Deposition date deposition_date2004-07-13
Structure title titleThe ternary von Willebrand Factor A1-glycoprotein Ibalpha-botrocetin complex
Keywords keywordsRossmann fold, LRR motif, C-type lectin fold, Protein-Protein complex, 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_guinier29.38
Radius of gyration Rg (electron density) rg_electron28.21
Forward intensity I(0) i0107500000.00
Molecular weight molecular_weight83262.0 kDa
Excluded volume excluded_volume104800 ų
Envelope volume envelope_volume125710 ų
Hydration-shell volume shell_volume36875 ų
Envelope diameter envelope_diameter97.4
Shell Rg shell_rg35.81
Envelope Rg envelope_rg28.04
Shape Rg shape_rg28.19
Total Rg total_rg29.01
Total atoms total_atoms5864
Residues n_residues731
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 dmax91.8
Rg (real space) rg_real29.26
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.0750e+08
I(0) uncertainty (real space) i0_real_error1.6680e+06
Rg (reciprocal space) rg_reciprocal29.32
I(0) (reciprocal space) i0_reciprocal107500000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27900000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1u0na_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.62 — vWA-like
Superfamily Superfamily superfamilyc.62.1 — vWA-like
Family Family familyc.62.1.1 — Integrin A (or I) domain
Domain ID domain_idd1u0nb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain
Domain ID domain_idd1u0nc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain
Domain ID domain_idd1u0nd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily Superfamily superfamilyc.10.2 — L domain-like
Family Family familyc.10.2.7 — Ngr ectodomain-like

CATH v4.4 (4 domains)

Domain ID domain_id1u0nA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily410 — von Willebrand factor, type A domain
Domain ID domain_id1u0nB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A
Domain ID domain_id1u0nC00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A
Domain ID domain_id1u0nD00
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor

8. Citations (1)

9. Files and Curves (10)