4c2a

Crystal Structure of High-Affinity von Willebrand Factor A1 domain with R1306Q and I1309V Mutations in Complex with High Affinity GPIb alpha

Method: X-RAY DIFFRACTION Dmax: 78.1 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1264–1471 Fragment:RESIDUES 1264-1471 Mutation:YES PLATELET GLYCOPROTEIN IB ALPHA CHAIN × 1 (P07359) CAC CACODYLATE ION × 1 ACT ACETATE ION × 1 CA CALCIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALS OF A1/VWD2-GPIBALPA/VWD2 COMPLEX APPEARED IN 12% PEG 8000, 0.1 M SODIUM CACODYLATE PH 6.5, 0.1 M CALCIUM ACETATE, AND 0.4 MG/ML RISTOCETIN (SIGMA-ALDRICH). THESE CRYSTALS WERE CRUSHED AND USED FOR SEEDING. CRYSTALS GREW IN 10 MG/ML COMPLEX, 14% PEG8000, 0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, AND 0.4 MG/ML RISTOCETIN. NEXT WE SOAKED THESE CRYSTALS IN 14% PEG8000, 0.2 M CALCIUM ACETATE, 0.1 SODIUM CACODYLATE, PH 6.5, AND 4 MG/ML RISTOCETIN. Resolution 2.08 Å R-free 0.189

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 2–209; UniProt 1264–1471

PLATELET GLYCOPROTEIN IB ALPHA CHAIN

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 17–306 Fragment:RESIDUES 17-306 Mutation:YES VON WILLEBRAND FACTOR × 1 (P04275) CAC CACODYLATE ION × 1 ACT ACETATE ION × 1 CA CALCIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALS OF A1/VWD2-GPIBALPA/VWD2 COMPLEX APPEARED IN 12% PEG 8000, 0.1 M SODIUM CACODYLATE PH 6.5, 0.1 M CALCIUM ACETATE, AND 0.4 MG/ML RISTOCETIN (SIGMA-ALDRICH). THESE CRYSTALS WERE CRUSHED AND USED FOR SEEDING. CRYSTALS GREW IN 10 MG/ML COMPLEX, 14% PEG8000, 0.2 M CALCIUM ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5, AND 0.4 MG/ML RISTOCETIN. NEXT WE SOAKED THESE CRYSTALS IN 14% PEG8000, 0.2 M CALCIUM ACETATE, 0.1 SODIUM CACODYLATE, PH 6.5, AND 4 MG/ML RISTOCETIN. Resolution 2.08 Å R-free 0.189

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–290; UniProt 17–306

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 4c2a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c2a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c2a
Deposition date deposition_date2013-08-16
Structure title titleCrystal Structure of High-Affinity von Willebrand Factor A1 domain with R1306Q and I1309V Mutations in Complex with High Affinity GPIb alpha
Keywords keywordsBLOOD CLOTTING, CELL ADHESION, A1, GPIBALPHA; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.56
Radius of gyration Rg (electron density) rg_electron23.38
Forward intensity I(0) i043554400.00
Molecular weight molecular_weight52980.0 kDa
Excluded volume excluded_volume67241 ų
Envelope volume envelope_volume79924 ų
Hydration-shell volume shell_volume28174 ų
Envelope diameter envelope_diameter80.7
Shell Rg shell_rg30.66
Envelope Rg envelope_rg23.45
Shape Rg shape_rg23.34
Total Rg total_rg24.39
Total atoms total_atoms3725
Residues n_residues468
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 dmax78.1
Rg (real space) rg_real24.43
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real4.3550e+07
I(0) uncertainty (real space) i0_real_error6.0190e+05
Rg (reciprocal space) rg_reciprocal24.46
I(0) (reciprocal space) i0_reciprocal43560000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.527
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7199000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4c2aa_
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_idd4c2ab_
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 (2 domains)

Domain ID domain_id4c2aA00
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_id4c2aB00
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)