SAXSdb — 9jtd

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

Angiotensin-converting enzyme

Vulpes vulpes

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 2 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 19–609	Not recorded	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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, SITTING DROP；291.15 K；0.2M Ammonium chloride, 20% w/v Polyethylene glycol 3350	Resolution 3.59 Å R-free 0.263
3	Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 19–609	Not recorded	Spike glycoprotein × 1 （A0A7D6PMV8） beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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, SITTING DROP；291.15 K；0.2M Ammonium chloride, 20% w/v Polyethylene glycol 3350	Resolution 3.59 Å R-free 0.263

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 9JTD	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8XYZ The structure of fox ACE2 and PT RBD complex Deposited 2024-01-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–613（613 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.96 Å
8XZB The structure of fox ACE2 and SARS-CoV RBD complex Deposited 2024-01-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–613（613 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å
8XZD The structure of fox ACE2 and Omicron BF.7 RBD complex Deposited 2024-01-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–613（613 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.47 Å
9JTE Crystal structure of SARS-CoV-2 receptor binding domain complexed with fox ACE2 Deposited 2024-10-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 19–609（591 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；0.2M Ammonium sulfate, 20% w/v Polyethylene glycol 3350	Resolution 3.66 Å R-free 0.249
9JTE Crystal structure of SARS-CoV-2 receptor binding domain complexed with fox ACE2 Deposited 2024-10-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 19–609（591 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；0.2M Ammonium sulfate, 20% w/v Polyethylene glycol 3350	Resolution 3.66 Å R-free 0.249

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A3Q7RAT9_VULVU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–592； UniProt 19–609

Spike glycoprotein

Pangolin coronavirus

UniProt A0A7D6PMV8

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain E； UniProt 329–522	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；291.15 K；0.2M Ammonium chloride, 20% w/v Polyethylene glycol 3350	Resolution 3.59 Å R-free 0.263
3	Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 329–522	Not recorded	Angiotensin-converting enzyme × 1 （A0A3Q7RAT9） beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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, SITTING DROP；291.15 K；0.2M Ammonium chloride, 20% w/v Polyethylene glycol 3350	Resolution 3.59 Å R-free 0.263

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A7D6PMV8_9BETC
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–194； UniProt 329–522

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	9jtd
Deposition date deposition_date	2024-10-04
Structure title title	Crystal structure of PCoV-GD receptor binding domain complexed with fox ACE2
Keywords keywords	PCoV-GD, receptor binding domain, fox ACE2, VIRAL PROTEIN; 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	31.27 Å
Radius of gyration Rg (electron density) rg_electron	30.80 Å
Forward intensity I(0) i0	133858000.00
Molecular weight molecular_weight	91861.0 kDa
Excluded volume excluded_volume	114560 Å³
Envelope volume envelope_volume	141840 Å³
Hydration-shell volume shell_volume	39502 Å³
Envelope diameter envelope_diameter	110.4 Å
Shell Rg shell_rg	37.08 Å
Envelope Rg envelope_rg	30.54 Å
Shape Rg shape_rg	30.76 Å
Total Rg total_rg	31.45 Å
Total atoms total_atoms	6479
Residues n_residues	786
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	105.3 Å
Rg (real space) rg_real	31.36 Å
Rg uncertainty (real space) rg_real_error	0.69 Å
I(0) (real space) i0_real	1.3390e+08
I(0) uncertainty (real space) i0_real_error	1.8960e+06
Rg (reciprocal space) rg_reciprocal	31.32 Å
I(0) (reciprocal space) i0_reciprocal	133900000.0000
Solution quality estimate total_estimate	0.6520
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	37.2 Å
Skewness Skewness skewness	0.501
Kurtosis Kurtosis kurtosis	0.036
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	25570000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.976; Smooth: 0.807

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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	Angiotensin-converting enzyme
Molecular weight formula_weight	68935.4 kDa
EC 编号 ec_number	3.4.-.-
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	6479

PSTEDLVNTFLEKFNYEAEELSYQSSLASWDYNTNISDENVQKMNNAGAKWSAFYEEQSKLAKTYPLEEIQDSTVKRQLRALQHSGSSVLSADKNQRLNTILNSMSTIYSTGKACNPSNPQECLLLEPGLDDIMENSKDYNERLWAWEGWRSEVGKQLRPLYEEYVALKNEMARANNYEDYGDYWRGDYEEEWENGYNYSRNQLIDDVEHTFTQIMPLYQHLHAYVRTKLMDTYPSYISPTGCLPAHLLGDMWGRFWTNLYPLTVPFGQKPNIDVTNAMVNQSWDARRIFKEAEKFFVSVGLPNMTQGFWENSMLTEPSDSRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPNHLKNIGLLPPSFFEDSETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKTWWEMKRNIVGVVEPVPHDETYCDPASLFHVANDYSFIRYYTRTIYQFQFQEALCQIAKHEGPLHKCDISNSSEAGQKLLEMLKLGKSKPWTYALEIVVGAKNMDVRPLLNYFEPLFTWLKEQNRNSFVGWNTDW

来源 Source

来源生物 organism	Vulpes vulpes
通用名 common_name	red fox
NCBI Class编号 ncbi_taxonomy_id	9627
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 polymer

Description description	Spike glycoprotein
Molecular weight formula_weight	21754.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

TNLCTFGEVFNATTFASVYAWNRKRISNCVADYSVLYNSTSFSTFKCYGVSPTKLNDLCFTNVYADSFVVRGDEVRQIAPGQTGRIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFHPTNGVGYQPYRVVVLSFELLNAPATVCG

来源 Source

来源生物 organism	Pangolin coronavirus
NCBI Class编号 ncbi_taxonomy_id	2708335
宿主生物 host_organism	Trichoplusia ni

Entity 3 Entity 3 branched

Description description	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	586.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

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

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8. Citations (1)

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Unit-cell length a length_a	193.952 Å
Unit-cell length b length_b	193.952 Å
Unit-cell length c length_c	151.024 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	16

Space group space_group	I 41 2 2
Space-group number int_tables_number	98
Crystal system crystal_system	—

Resolution resolution	3.590 Å
Low-resolution limit resolution_low	33.070 Å
R factor r_factor	0.2306
R_work r_work	0.2289
R_free r_free	0.2628

fit	/app/data/saxs_computation/jt/9jtd/9jtd.fit
pddf	/app/data/pr_computation/jt/9jtd/9jtd.pr.out
profile	/app/data/saxs_computation/jt/9jtd/9jtd.dat

Crystal structure of PCoV-GD receptor binding domain complexed with fox ACE2

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

Angiotensin-converting enzyme

State in the Current Structure

Other States of the Same Protein in the Database

Spike glycoprotein

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 (4)

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 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)