1p9a

Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution

Method: X-RAY DIFFRACTION Dmax: 74.8 Å Quality: GOOD

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

Platelet glycoprotein Ib alpha chain precursor

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 17–306 Fragment:N-Terminal Domain Mutation:C65A ;beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;PEG 6000, Sodium Nitrate, Sodium Acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.70 Å R-free 0.224

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 GPBA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; 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 1p9a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p9a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p9a
Deposition date deposition_date2003-05-09
Structure title titleCrystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution
Keywords keywordsPlatelet Receptors, Glycocalicin, Leucine Rich Repeats, 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_guinier21.71
Radius of gyration Rg (electron density) rg_electron20.83
Forward intensity I(0) i014868600.00
Molecular weight molecular_weight30215.0 kDa
Excluded volume excluded_volume38378 ų
Envelope volume envelope_volume45391 ų
Hydration-shell volume shell_volume19053 ų
Envelope diameter envelope_diameter76.1
Shell Rg shell_rg26.52
Envelope Rg envelope_rg21.07
Shape Rg shape_rg20.78
Total Rg total_rg21.82
Total atoms total_atoms2127
Residues n_residues266
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 dmax74.8
Rg (real space) rg_real21.77
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.4870e+07
I(0) uncertainty (real space) i0_real_error2.0740e+05
Rg (reciprocal space) rg_reciprocal21.76
I(0) (reciprocal space) i0_reciprocal14870000.0000
Solution quality estimate total_estimate0.8564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.436
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1809000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1p9ag_
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 (1 domains)

Domain ID domain_id1p9aG00
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)