1qyy

Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution

Method: X-RAY DIFFRACTION Dmax: 105.0 Å Quality: REASONABLE

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

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 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 17–306 Fragment:N-Terminal Domain Mutation:C65A ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 PT PLATINUM (II) ION × 2 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 2.80 Å R-free 0.282
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain G; UniProt 17–306 Fragment:N-Terminal Domain Mutation:C65A PT PLATINUM (II) ION × 1 NAG 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 2.80 Å R-free 0.282

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 GPBA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–290; UniProt 17–306 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 1qyy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qyy
Deposition date deposition_date2003-09-12
Structure title titleCrystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution
Keywords keywordsPlatelet Receptors, Glycocalicin, Leucine Rich Repeats, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.46
Radius of gyration Rg (electron density) rg_electron30.49
Forward intensity I(0) i056526800.00
Molecular weight molecular_weight60484.0 kDa
Excluded volume excluded_volume76225 ų
Envelope volume envelope_volume96198 ų
Hydration-shell volume shell_volume28466 ų
Envelope diameter envelope_diameter111.1
Shell Rg shell_rg34.72
Envelope Rg envelope_rg30.68
Shape Rg shape_rg30.46
Total Rg total_rg31.00
Total atoms total_atoms4221
Residues n_residues532
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 dmax105.0
Rg (real space) rg_real30.77
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real5.6530e+07
I(0) uncertainty (real space) i0_real_error8.7570e+05
Rg (reciprocal space) rg_reciprocal30.64
I(0) (reciprocal space) i0_reciprocal56520000.0000
Solution quality estimate total_estimate0.6093
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.562
Kurtosis Kurtosis kurtosis-0.321
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13160000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.702; Stabil: 1.000; Sysdev: 0.077; Positv: 1.000; Valcen: 0.675; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1qyya_
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_idd1qyyg_
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_id1qyyA00
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_id1qyyG00
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)