SAXSdb — 7rtx

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

Actophorin

Acanthamoeba castellanii

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 2–138	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；10 mg/mL protein, 0.1 M MOPS, 16% Polyethylene glycol (8,000)	Resolution 1.65 Å R-free 0.223

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 7RTX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AHQ RECOMBINANT ACTOPHORIN Deposited 1997-04-10	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–137（137 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；20-25% PEG 8000, 100MM HEPES (PH7.5), 10% ISOPROPANOL, 1MM DTT	Resolution 2.30 Å R-free 0.320
1CNU PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA Deposited 1999-05-24	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–137（136 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.0	Resolution 2.25 Å R-free 0.304
7SOG Thermostable actophorin Deposited 2021-10-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–135（134 aa）	Mutation：S2P, H21K, Q22K, T27I, M30L, A32D, S33D, H41K, K53L, S54A, R59N, Q71E, T81V, T99A, T101S, S104A, V110D, A122D, S130K	NI NICKEL (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；PEG 8000, NISO4, MES pH6.5	Resolution 1.74 Å R-free 0.225
7SOG Thermostable actophorin Deposited 2021-10-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–135（134 aa）	Mutation：S2P, H21K, Q22K, T27I, M30L, A32D, S33D, H41K, K53L, S54A, R59N, Q71E, T81V, T99A, T101S, S104A, V110D, A122D, S130K	NI NICKEL (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；PEG 8000, NISO4, MES pH6.5	Resolution 1.74 Å R-free 0.225

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

View Construct and Data Evidence

UniProt name	ACTP_ACACA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–137； UniProt 2–138

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	7rtx
Deposition date deposition_date	2021-08-16
Structure title title	Actophorin grown in microgravity
Keywords keywords	microgravity, MOTOR PROTEIN; MOTOR 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	15.72 Å
Radius of gyration Rg (electron density) rg_electron	14.27 Å
Forward intensity I(0) i0	4524030.00
Molecular weight molecular_weight	14974.0 kDa
Excluded volume excluded_volume	18663 Å³
Envelope volume envelope_volume	20969 Å³
Hydration-shell volume shell_volume	12567 Å³
Envelope diameter envelope_diameter	52.6 Å
Shell Rg shell_rg	19.98 Å
Envelope Rg envelope_rg	14.66 Å
Shape Rg shape_rg	14.21 Å
Total Rg total_rg	15.55 Å
Total atoms total_atoms	1290
Residues n_residues	133
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	55.9 Å
Rg (real space) rg_real	15.65 Å
Rg uncertainty (real space) rg_real_error	0.39 Å
I(0) (real space) i0_real	4.5240e+06
I(0) uncertainty (real space) i0_real_error	5.9950e+04
Rg (reciprocal space) rg_reciprocal	15.66 Å
I(0) (reciprocal space) i0_reciprocal	4524000.0000
Solution quality estimate total_estimate	0.7627
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	55.2 Å
Skewness Skewness skewness	0.231
Kurtosis Kurtosis kurtosis	-0.176
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1035000.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.646; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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Unit-cell length a length_a	39.810 Å
Unit-cell length b length_b	45.800 Å
Unit-cell length c length_c	69.310 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	orthorhombic

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	34.660 Å
R factor r_factor	0.1902
R_work r_work	0.1880
R_free r_free	0.2233

Description description	Actophorin
Molecular weight formula_weight	15444.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1518

Actophorin grown in microgravity

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

Actophorin

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Acanthamoeba castellanii
通用名 common_name	Amoeba
NCBI Class编号 ncbi_taxonomy_id	5755
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	108

fit	/app/data/saxs_computation/rt/7rtx/7rtx.fit
pddf	/app/data/pr_computation/rt/7rtx/7rtx.pr.out
profile	/app/data/saxs_computation/rt/7rtx/7rtx.dat