1m0z

Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha

Method: X-RAY DIFFRACTION Dmax: 114.4 Å Quality: GOOD

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

Glycoprotein Ib alpha

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 17–306 Fragment:von Willebrand Factor binding domain Mutation:N21Q N159Q No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.2;301 K;ammonium sulfate, lithium sulfate, CAPS, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 301K Resolution 1.85 Å R-free 0.216
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 17–306 Fragment:von Willebrand Factor binding domain Mutation:N21Q N159Q No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.2;301 K;ammonium sulfate, lithium sulfate, CAPS, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 301K Resolution 1.85 Å R-free 0.216

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP1BA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–290; UniProt 17–306 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 1m0z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m0z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m0z
Deposition date deposition_date2002-06-16
Structure title titleCrystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha
Keywords keywordsleucine-rich repeat, hemostasis, 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_guinier31.76
Radius of gyration Rg (electron density) rg_electron31.40
Forward intensity I(0) i050580000.00
Molecular weight molecular_weight58410.0 kDa
Excluded volume excluded_volume74244 ų
Envelope volume envelope_volume93681 ų
Hydration-shell volume shell_volume27307 ų
Envelope diameter envelope_diameter122.5
Shell Rg shell_rg34.71
Envelope Rg envelope_rg31.73
Shape Rg shape_rg31.41
Total Rg total_rg31.67
Total atoms total_atoms4113
Residues n_residues525
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 dmax114.4
Rg (real space) rg_real32.15
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real5.0580e+07
I(0) uncertainty (real space) i0_real_error8.6950e+05
Rg (reciprocal space) rg_reciprocal31.99
I(0) (reciprocal space) i0_reciprocal50570000.0000
Solution quality estimate total_estimate0.8131
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.561
Kurtosis Kurtosis kurtosis-0.267
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8263000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.632; Smooth: 0.946

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_idd1m0za_
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
Domain ID domain_idd1m0zb_
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_id1m0zA00
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
Domain ID domain_id1m0zB00
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)