1h9v

Human Fc-gamma-Receptor IIa (FcgRIIa), monoclinic

Method: X-RAY DIFFRACTION Dmax: 64.8 Å Quality: GOOD

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

LOW AFFINITY IMMUNOGLOBULIN GAMMA FC 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 37–208 Fragment:IMMUNOGLOBULIN G BINDING DOMAIN RESIDUE 5-177 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;0.2M NAOAC PH 4.6, 26% PEG 8000 Resolution 3.00 Å

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 FCGA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–172; UniProt 37–208

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 1h9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1h9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1h9v
Deposition date deposition_date2001-03-21
Structure title titleHuman Fc-gamma-Receptor IIa (FcgRIIa), monoclinic
Keywords keywordsIMMUNE SYSTEM, MEMBRANE PROTEIN, FCR, FC-RECEPTOR, IMMUNOGLOBULIN, FCGR, FC-GAMMA-R; IMMUNE SYSTEM, MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.05
Radius of gyration Rg (electron density) rg_electron18.23
Forward intensity I(0) i07099960.00
Molecular weight molecular_weight19320.0 kDa
Excluded volume excluded_volume24072 ų
Envelope volume envelope_volume29369 ų
Hydration-shell volume shell_volume14267 ų
Envelope diameter envelope_diameter65.0
Shell Rg shell_rg23.19
Envelope Rg envelope_rg18.43
Shape Rg shape_rg18.21
Total Rg total_rg19.10
Total atoms total_atoms1364
Residues n_residues172
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 dmax64.8
Rg (real space) rg_real19.06
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real7.1000e+06
I(0) uncertainty (real space) i0_real_error8.1610e+04
Rg (reciprocal space) rg_reciprocal19.06
I(0) (reciprocal space) i0_reciprocal7100000.0000
Solution quality estimate total_estimate0.8816
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha1938000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.905; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1h9va1
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_idd1h9va2
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_id1h9vA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1h9vA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)