SAXSdb — 6y6q

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

Envelope polyprotein

Andes orthohantavirus

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 Homooligomer Protein × 3 其他Polymer 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 652–1107	Not recorded	;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；16% (w/v) PEG 4000, 10% (v/v) 2-propanol, 0.2M (NH4)2SO4, 0.1M Hepes pH 7.5	Resolution 2.70 Å R-free 0.287

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 6Y6Q	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6YRB Crystal structure of the tetramerization domain of the glycoprotein Gn (Andes virus) at pH 7.5 Deposited 2020-04-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 375–484（110 aa） Chain B 375–484（110 aa）	Not recorded	IOD IODIDE ION × 24	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2M NaCl, 0.1M Hepes 7.5, 35% MPD	Resolution 2.35 Å R-free 0.266
6YRQ Crystal structure of the tetramerization domain of the glycoprotein Gn (Andes virus) at pH 4.6 Deposited 2020-04-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 4 PDB declaration: octameric	Chain A 375–484（110 aa） Chain B 375–484（110 aa） Chain C 375–484（110 aa） Chain D 375–484（110 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2M CaCl2, 0.1M Na-acetate 4.6, 30% MPD	Resolution 1.90 Å R-free 0.230
8DBZ CryoEM structure of Hantavirus ANDV Gn(H) protein complex with 2Fabs ANDV-5 and ANDV-34 Deposited 2022-06-15	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 22–374（353 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
9P3I High-resolution in situ ANDV single tetramer structure Deposited 2025-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–651（651 aa） Chain B 652–1138（487 aa） Chain C 1–651（651 aa） Chain D 652–1138（487 aa） Chain E 1–651（651 aa） Chain F 652–1138（487 aa） Chain G 1–651（651 aa） Chain H 652–1138（487 aa）	Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.35 Å
9P3L Structure of ANDV dimer of tetramer at conformation III Deposited 2025-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–651（651 aa） Chain B 652–1138（487 aa） Chain C 1–651（651 aa） Chain D 652–1138（487 aa） Chain E 1–651（651 aa） Chain F 652–1138（487 aa） Chain G 1–651（651 aa） Chain H 652–1138（487 aa） Chain I 1–651（651 aa） Chain J 652–1138（487 aa） Chain K 1–651（651 aa） Chain L 652–1138（487 aa） Chain M 1–651（651 aa） Chain N 652–1138（487 aa） Chain O 1–651（651 aa） Chain P 652–1138（487 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.37 Å
9P3M Structure of the ANDV dimer of tetramer at conformation II Deposited 2025-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–651（651 aa） Chain B 652–1138（487 aa） Chain C 1–651（651 aa） Chain D 652–1138（487 aa） Chain E 1–651（651 aa） Chain F 652–1138（487 aa） Chain G 1–651（651 aa） Chain H 652–1138（487 aa） Chain I 1–651（651 aa） Chain J 652–1138（487 aa） Chain K 1–651（651 aa） Chain L 652–1138（487 aa） Chain M 1–651（651 aa） Chain N 652–1138（487 aa） Chain O 1–651（651 aa） Chain P 652–1138（487 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
9P3X Structure of the ANDV dimer of tetramer at conformation I Deposited 2025-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–651（651 aa） Chain B 652–1138（487 aa） Chain C 1–651（651 aa） Chain D 652–1138（487 aa） Chain E 1–651（651 aa） Chain F 652–1138（487 aa） Chain G 1–651（651 aa） Chain H 652–1138（487 aa） Chain I 1–651（651 aa） Chain J 652–1138（487 aa） Chain K 1–651（651 aa） Chain L 652–1138（487 aa） Chain M 1–651（651 aa） Chain N 652–1138（487 aa） Chain O 1–651（651 aa） Chain P 652–1138（487 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
9P3Y Andes virus glycoprotein tetramer in complex with ADI-65534 Fab Deposited 2025-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–651（651 aa） Chain B 652–1138（487 aa） Chain C 1–651（651 aa） Chain D 652–1138（487 aa） Chain E 1–651（651 aa） Chain F 652–1138（487 aa） Chain G 1–651（651 aa） Chain H 652–1138（487 aa）	Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L Mutation：V535K Mutation：S1096L	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å

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

View Construct and Data Evidence

UniProt name	Q9E006_9VIRU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–458； UniProt 652–1107

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	6y6q
Deposition date deposition_date	2020-02-27
Structure title title	Structure of Andes virus envelope glycoprotein Gc in postfusion conformation
Keywords keywords	class-II fusion protein hantavirus bunyavirus, VIRAL PROTEIN, postfusion conformation; VIRAL PROTEIN
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	29.87 Å
Radius of gyration Rg (electron density) rg_electron	29.97 Å
Forward intensity I(0) i0	35120100.00
Molecular weight molecular_weight	44364.0 kDa
Excluded volume excluded_volume	54790 Å³
Envelope volume envelope_volume	72567 Å³
Hydration-shell volume shell_volume	23025 Å³
Envelope diameter envelope_diameter	116.1 Å
Shell Rg shell_rg	32.26 Å
Envelope Rg envelope_rg	30.69 Å
Shape Rg shape_rg	29.95 Å
Total Rg total_rg	30.26 Å
Total atoms total_atoms	3094
Residues n_residues	396
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	110.4 Å
Rg (real space) rg_real	30.34 Å
Rg uncertainty (real space) rg_real_error	1.53 Å
I(0) (real space) i0_real	3.5120e+07
I(0) uncertainty (real space) i0_real_error	6.1830e+05
Rg (reciprocal space) rg_reciprocal	30.14 Å
I(0) (reciprocal space) i0_reciprocal	35110000.0000
Solution quality estimate total_estimate	0.7736
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.1 Å
Skewness Skewness skewness	0.691
Kurtosis Kurtosis kurtosis	0.009
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3675000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.579; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.413; Smooth: 0.903

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Envelope polyprotein
Molecular weight formula_weight	54270.9 kDa
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	3098

RSETPLMESGWSDTAHGVGEIPMKTDLELDFSLPSSSSYSYRRKLTNPANKEESIPFHFQMEKQVIHAEIQPLGHWMDATFNIKTAFHCYGACQKYSYPWQTSKCFFEKDYQYETGWGCNPGDCPGVGTGCTACGVYLDKLKSVGKAYKIISLKYTRKVCIQLGTEQTCKHIDANDCLVTPSVKVCIVGTVSKLQPSDTLLFLGPLEQGGIILKQWCTTSCAFGDPGDIMSTPSGMRCPEHTGSFRKICGFATTPVCEYQGNTISGYKRMMATKDSFQSFNLTEPHITTNKLEWIDPDGNTRDHVNLVLNRDVSFQDLSDNPCKVDLHTQAIEGAWGSGVGFTLTCTVGLTECPSFMTSIKACDLAMCYGSTVTNLARGSNTVKVVGKGGHSGSSFKCCHDTDCSSEGLLASAPHLERVTGFNQIDSDKVYDDGAPPCTFKCWFTKSGEWLLGILNGNGPFEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK

来源 Source

来源生物 organism	Andes orthohantavirus
NCBI Class编号 ncbi_taxonomy_id	1980456
宿主生物 host_organism	Drosophila melanogaster

Entity 2 Entity 2 branched

Description description	;alpha-D-mannopyranose-(1-6)-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	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	4

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8. Citations (1)

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Unit-cell length a length_a	92.647 Å
Unit-cell length b length_b	92.647 Å
Unit-cell length c length_c	318.545 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	39.803 Å
R factor r_factor	0.2368
R_work r_work	0.2341
R_free r_free	0.2869

fit	/app/data/saxs_computation/y6/6y6q/6y6q.fit
pddf	/app/data/pr_computation/y6/6y6q/6y6q.pr.out
profile	/app/data/saxs_computation/y6/6y6q/6y6q.dat

Structure of Andes virus envelope glycoprotein Gc in postfusion conformation

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

Envelope polyprotein

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