8cha

Fc gamma RIIa 27W/131H variant ectodomain

Method: X-RAY DIFFRACTION D_max: 65.7 Å Quality: GOOD

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

Low affinity immunoglobulin gamma Fc region receptor II-a

Homo sapiens

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 1–209	Mutation：Q27W	;alpha-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 FLC CITRATE ANION × 1 PO4 PHOSPHATE ION × 3 16P 3,6,9,12,15,18-HEXAOXAICOSANE × 1 PGE TRIETHYLENE GLYCOL × 1 DXE 1,2-DIMETHOXYETHANE × 1 FWN 2-[2-(2-ethoxyethoxy)ethoxy]ethanol × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 4.2；293.15 K；0.1M sodium phosphate citrate, pH4.2, 41% (v/v) PEG 300	Resolution 1.81 Å R-free 0.225

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.

Other PDB	Difference from Current Entry 8CHA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1FCG ECTODOMAIN OF HUMAN FC GAMMA RECEPTOR, FCGRIIA Deposited 1999-04-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 34–207（174 aa） Fragment：EXTRACELLULAR DOMAINS	Mutation：S88F, R134H	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.6；HANGING DROP VAPOUR DIFFUSION WITH EQUAL VOLUMES OF FC(GAMMA)RIIA AT 6 MG/ML AND MOTHER LIQUOR (0.2 M AMMONIUM ACETATE, 30% W/V PEG 4000, 0.1 M SODIUM CITRATE PH 5.6) MIXED IN 3 MICRO L DROPLETS AND ALLOWED TO EQUILIBRATE AT 22 C FOR 3-9 DAYS.	Resolution 2.00 Å R-free 0.242
1H9V Human Fc-gamma-Receptor IIa (FcgRIIa), monoclinic Deposited 2001-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–208（172 aa） Fragment：IMMUNOGLOBULIN G BINDING DOMAIN RESIDUE 5-177	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；0.2M NAOAC PH 4.6, 26% PEG 8000	Resolution 3.00 Å
3D5O Structural recognition and functional activation of FcrR by innate pentraxins Deposited 2008-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain F 37–207（171 aa）	Not recorded	SO4 SULFATE ION × 16 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；2.0 M NH4SO4, 5% iso-propanol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.279
3RY4 1.5 Angstrom resolution structure of glycosylated fcgammariia (low-responder polymorphism) Deposited 2011-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–206（170 aa） Fragment：EXTRACELLULAR DOMAIN, residues 37-206	Mutation：S88P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 5.6；30% (W/V) PEG 4000, 0.2M AMMONIUM ACETATE, 0.1M SODIUM CITRATE, PH 5.60, VAPOR DIFFUSION, TEMPERATURE 291.0K	Resolution 1.50 Å R-free 0.230
3RY5 Three-dimensional structure of glycosylated fcgammariia (high-responder polymorphism) Deposited 2011-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–206（170 aa） Fragment：EXTRACELLULAR DOMAIN, residues 114-327	Mutation：H134R	No recorded non-water small molecule	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
3RY6 Complex of fcgammariia (CD32) and the FC of human IGG1 Deposited 2011-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 40–206（167 aa） Fragment：UNP residues 40-206	Not recorded	GOL GLYCEROL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.4；20% (W/V) PEG 3350, 5MM TRIS, 0.15M NACL, 2MM MOPS, 0.2M TRI-POTASSIUM ACETATE, PH 7.40, VAPOR DIFFUSION, TEMPERATURE 291.0K	Resolution 3.80 Å R-free 0.426
9MCX CRYSTAL STRUCTURE OF HUMAN IGG1 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT Deposited 2024-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 37–209（173 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；25% PEG 2000 MME, 0.1 M HEPES pH 7.5	Resolution 2.38 Å R-free 0.234
9N5P CRYSTAL STRUCTURE OF HUMAN IGG2 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT Deposited 2025-02-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 37–209（173 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1 M HEPES pH 7.5, 25% PEG 2000 MME	Resolution 2.01 Å R-free 0.232

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 1–209； UniProt 1–209

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8cha
Deposition date deposition_date	2023-02-07
Structure title title	Fc gamma RIIa 27W/131H variant ectodomain
Keywords keywords	FcgR, Fc receptor, antibody receptor, inflammation, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	18.91 Å
Radius of gyration Rg (electron density) rg_electron	18.23 Å
Forward intensity I(0) i0	7870560.00
Molecular weight molecular_weight	20404.0 kDa
Excluded volume excluded_volume	25382 Å³
Envelope volume envelope_volume	30179 Å³
Hydration-shell volume shell_volume	14610 Å³
Envelope diameter envelope_diameter	64.2 Å
Shell Rg shell_rg	23.19 Å
Envelope Rg envelope_rg	18.51 Å
Shape Rg shape_rg	18.14 Å
Total Rg total_rg	19.28 Å
Total atoms total_atoms	2735
Residues n_residues	167
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	65.7 Å
Rg (real space) rg_real	18.93 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	7.8710e+06
I(0) uncertainty (real space) i0_real_error	1.0300e+05
Rg (reciprocal space) rg_reciprocal	18.93 Å
I(0) (reciprocal space) i0_reciprocal	7871000.0000
Solution quality estimate total_estimate	0.8656
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.2 Å
Skewness Skewness skewness	0.345
Kurtosis Kurtosis kurtosis	-0.420
Angular range angular_range	— – 0.4200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2004000.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.881; Smooth: 0.997

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	Low affinity immunoglobulin gamma Fc region receptor II-a
Molecular weight formula_weight	23440.4 kDa
Mutation mutation	Q27W
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2934

MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCWGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 branched

Description description	;alpha-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 ;
Molecular weight formula_weight	748.7 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CITRATE ANION
Molecular weight formula_weight	189.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	3,6,9,12,15,18-HEXAOXAICOSANE
Molecular weight formula_weight	294.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	1,2-DIMETHOXYETHANE
Molecular weight formula_weight	90.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 non-polymer

Description description	2-[2-(2-ethoxyethoxy)ethoxy]ethanol
Molecular weight formula_weight	178.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	111

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8. Citations (1)

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Unit-cell length a length_a	49.931 Å
Unit-cell length b length_b	76.526 Å
Unit-cell length c length_c	108.279 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.810 Å
Low-resolution limit resolution_low	41.817 Å
R factor r_factor	0.1944
R_work r_work	0.1928
R_free r_free	0.2247

fit	/app/data/saxs_computation/ch/8cha/8cha.fit
pddf	/app/data/pr_computation/ch/8cha/8cha.pr.out
profile	/app/data/saxs_computation/ch/8cha/8cha.dat