SAXSdb — 9n5p

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

Isoform 1 of Immunoglobulin heavy constant gamma 2

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 Heteromer Protein × 3 其他Polymer 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 195–417 Chain B； UniProt 195–417	Not recorded	Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant × 1 （P12318） ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 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

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 9N5P	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2HFG Crystal structure of hBR3 bound to CB3s-Fab Deposited 2006-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 1–194（194 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions Drops contained 2.1 microliters protein solution (pH 6.5) and 2.9 microliters of (0.1M citric acid pH 3.0, 24% PEG 3350, and 0.1 M Praseodymium (III) acetate) over a reservoir of 24% PEG 3350. pH of final drop ~4.5.	Resolution 2.61 Å R-free 0.252

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6N093_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–223； UniProt 195–417 Author chain B； PDBConstruct 1–223； UniProt 195–417

Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant

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	Other combination Heteromer Protein × 3 其他Polymer 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 37–209	Not recorded	Isoform 1 of Immunoglobulin heavy constant gamma 2 × 2 （Q6N093） ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 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

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 9N5P	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 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 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 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
8CHA Fc gamma RIIa 27W/131H variant ectodomain Deposited 2023-02-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–209（209 aa）	Mutation：Q27W	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
9MCX CRYSTAL STRUCTURE OF HUMAN IGG1 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT Deposited 2024-12-05	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

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	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–173； UniProt 37–209

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9n5p
Deposition date deposition_date	2025-02-04
Structure title title	CRYSTAL STRUCTURE OF HUMAN IGG2 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT
Keywords keywords	IMMUNOGLOBULIN, IGG2, IMMUNE SYSTEM, IMMUNOGLOBULIN-LIKE BETA SANDWICH, FC FRAGMENT, FC GAMMA RECEPTOR IIA, CD32A; 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	32.79 Å
Radius of gyration Rg (electron density) rg_electron	32.03 Å
Forward intensity I(0) i0	81131000.00
Molecular weight molecular_weight	70889.0 kDa
Excluded volume excluded_volume	88600 Å³
Envelope volume envelope_volume	121180 Å³
Hydration-shell volume shell_volume	33068 Å³
Envelope diameter envelope_diameter	117.4 Å
Shell Rg shell_rg	37.13 Å
Envelope Rg envelope_rg	31.38 Å
Shape Rg shape_rg	32.02 Å
Total Rg total_rg	32.50 Å
Total atoms total_atoms	4989
Residues n_residues	594
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	112.4 Å
Rg (real space) rg_real	32.94 Å
Rg uncertainty (real space) rg_real_error	1.12 Å
I(0) (real space) i0_real	8.1130e+07
I(0) uncertainty (real space) i0_real_error	1.3970e+06
Rg (reciprocal space) rg_reciprocal	32.88 Å
I(0) (reciprocal space) i0_reciprocal	81130000.0000
Solution quality estimate total_estimate	0.8624
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.2 Å
Skewness Skewness skewness	0.441
Kurtosis Kurtosis kurtosis	-0.095
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6969000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.932; Smooth: 0.830

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Isoform 1 of Immunoglobulin heavy constant gamma 2
Molecular weight formula_weight	25112.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5280

VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

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 polymer

Description description	Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant
Molecular weight formula_weight	19410.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

APPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPS

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 3 Entity 3 branched

Description description	;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	732.7 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 branched

Description description	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1463.3 kDa
Source method src_method	man
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	281

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8. Citations (1)

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Unit-cell length a length_a	161.853 Å
Unit-cell length b length_b	66.949 Å
Unit-cell length c length_c	71.179 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.18 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.010 Å
Low-resolution limit resolution_low	27.550 Å
R factor r_factor	0.1971
R_work r_work	0.1952
R_free r_free	0.2324

fit	/app/data/saxs_computation/n5/9n5p/9n5p.fit
pddf	/app/data/pr_computation/n5/9n5p/9n5p.pr.out
profile	/app/data/saxs_computation/n5/9n5p/9n5p.dat

CRYSTAL STRUCTURE OF HUMAN IGG2 FC FRAGMENT-FC-GAMMA RECEPTOR IIA COMPLEX H131 VARIANT

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

Isoform 1 of Immunoglobulin heavy constant gamma 2

State in the Current Structure

Other States of the Same Protein in the Database

Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 branched

Entity 4 Entity 4 branched

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)