3ry5

Three-dimensional structure of glycosylated fcgammariia (high-responder polymorphism)

Method: X-RAY DIFFRACTION Dmax: 67.2 Å Quality: GOOD

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

LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR II-A

Homo sapiens

UniProt P12318

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 37–206 Fragment:EXTRACELLULAR DOMAIN, residues 114-327 Mutation:H134R No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;30% (W/V) PEG 4000, 0.2M AMMONIUM SULFATE, PH 7.50, VAPOR DIFFUSION, TEMPERATURE 291.0K Resolution 2.30 Å R-free 0.275

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCG2A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–170; UniProt 37–206

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 3ry5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ry5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ry5
Deposition date deposition_date2011-05-11
Structure title titleThree-dimensional structure of glycosylated fcgammariia (high-responder polymorphism)
Keywords keywords;FC RECEPTOR, CD32, IMMUNOGLOBULIN SUPERFAMILY, HIGH RESPONDER POLYMORPHISM, CELL MEMBRANE, IGG-BINDING PROTEIN, IMMUNOGLOBULIN DOMAIN, MEMBRANE, RECEPTOR, TRANSMEMBRANE, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.80
Radius of gyration Rg (electron density) rg_electron17.99
Forward intensity I(0) i07007300.00
Molecular weight molecular_weight19123.0 kDa
Excluded volume excluded_volume23802 ų
Envelope volume envelope_volume27853 ų
Hydration-shell volume shell_volume13785 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg22.98
Envelope Rg envelope_rg18.36
Shape Rg shape_rg17.98
Total Rg total_rg18.85
Total atoms total_atoms1350
Residues n_residues170
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 dmax67.2
Rg (real space) rg_real18.84
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real7.0070e+06
I(0) uncertainty (real space) i0_real_error8.7990e+04
Rg (reciprocal space) rg_reciprocal18.83
I(0) (reciprocal space) i0_reciprocal7007000.0000
Solution quality estimate total_estimate0.7779
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1679000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.827; Smooth: 0.000

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_idd3ry5a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd3ry5a2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains

CATH v4.4 (2 domains)

Domain ID domain_id3ry5A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3ry5A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)