1acx

ACTINOXANTHIN STRUCTURE AT THE ATOMIC LEVEL (RUSSIAN)

Method: X-RAY DIFFRACTION D_max: 47.5 Å Quality: GOOD

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

ACTINOXANTHIN

Streptomyces globisporus

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 34–143	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.00 Å

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	ATXA_STRGL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–108； UniProt 34–143

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	1acx
Deposition date deposition_date	1982-12-17
Structure title title	ACTINOXANTHIN STRUCTURE AT THE ATOMIC LEVEL (RUSSIAN)
Keywords keywords	ANTIBACTERIAL PROTEIN; ANTIBACTERIAL 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	14.30 Å
Radius of gyration Rg (electron density) rg_electron	13.13 Å
Forward intensity I(0) i0	2538090.00
Molecular weight molecular_weight	10280.0 kDa
Excluded volume excluded_volume	12513 Å³
Envelope volume envelope_volume	14309 Å³
Hydration-shell volume shell_volume	9699 Å³
Envelope diameter envelope_diameter	44.8 Å
Shell Rg shell_rg	18.21 Å
Envelope Rg envelope_rg	13.29 Å
Shape Rg shape_rg	13.12 Å
Total Rg total_rg	14.27 Å
Total atoms total_atoms	721
Residues n_residues	108
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	47.5 Å
Rg (real space) rg_real	14.25 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	2.5380e+06
I(0) uncertainty (real space) i0_real_error	3.1370e+04
Rg (reciprocal space) rg_reciprocal	14.25 Å
I(0) (reciprocal space) i0_reciprocal	2538000.0000
Solution quality estimate total_estimate	0.8824
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.2 Å
Skewness Skewness skewness	0.222
Kurtosis Kurtosis kurtosis	-0.425
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	599200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.995

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1acxa_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.7 — Actinoxanthin-like
Family Family family	b.1.7.1 — Actinoxanthin-like

CATH v4.4 (1 domains)

Domain ID domain_id	1acxA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	230 — Neocarzinostatin-like

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8. Citations (22)

Actinoxanthin Structure at the Atomic Level (Russian)

Bioorg.Khim. (1982)

PMID: -1 PRIMARY

X-Ray Investigation of Three Dimensional Structure of Actinoxanthin

Chemistry of Peptides and Proteins (1982)

Three-Dimensional Structure of Actinoxanthin. Iv. A 2.5-Angstroms Resolution

Biopolymers (1982)

High Resolution X-Ray Structural Investigation of Actinoxanthin

Sov.Phys.Crystallogr.(Engl.Transl.) (1982)

Three-Dimensional Structure of Actinoxanthin. III. A 4-Angstroms Resolution

Biopolymers (1981)

X-Ray Diffraction Studies of Actinoxanthine at High Resolution (Russian)

Kristallografiya (1981)

Effect of Actinoxanthine, an Antitumor Antibiotic on Cells Cultivated in Vitro

Antibiotiki(Moscow) (1981)

Actinoxanthine Structure in Crystal and Aqueous Solution (Russian)

Bioorg.Khim. (1981)

The Spatial Structure of Actinoxanthin. II. Localization of the Heavy Atoms in Isomorphic Derivatives by Direct X-Ray Methods

Sov.J.Bioorg.Chem.(Engl.Transl.) (1981)

Three-Dimensional Structure of Actinoxanthine at 2.8 Angstroms Resolution (Russian)

Bioorg.Khim. (1980)

Three-Dimensional Structure of Actinoxanthin. I. Crystallization and Preliminary X-Ray Structural Results

Sov.J.Bioorg.Chem.(Engl.Transl.) (1980)

;Three Dimensional Structure of Actinoxanthin. II. The Location of Heavy Atom Sites in Isomorphous Derivatives by X-Ray Direct Methods (Russian) ;

Bioorg.Khim. (1980)

Three-Dimensional Structure of Actinoxanthine. I. Crystallization and Preliminary X-Ray Data (Russian)

Bioorg.Khim. (1979)

Chemical Studies on Actinoxanthin

J.Antibiot. (1976)

Actinoxanthin. Vii. Location of Disulfide Bonds in Actinoxanthin (Russian)

Bioorg.Khim. (1976)

Actinoxanthin. Vii. Determination of the Positions of the Disulfide Bonds

Sov.J.Bioorg.Chem.(Engl.Transl.) (1976)

Actinoxanthin. Vi. Peptides of Tryptic Hydrolysis. Amino-Acid Sequence of Actinoxanthin

Sov.J.Bioorg.Chem.(Engl.Transl.) (1976)

Actinoxanthin. V. The Peptides of a Thermolysin Hydrolyzate of Actinoxanthin

Sov.J.Bioorg.Chem.(Engl.Transl.) (1976)

Actinoxanthin. Iv. Peptides of a Chymotryptic Hydrolysate of Actinoxanthin

Sov.J.Bioorg.Chem.(Engl.Transl.) (1976)

Actinoxanthin. Vi. Tryptic Peptides and Amino Acid Sequence of Actinoxanthin (Russian)

Bioorg.Khim. (1975)

Actinoxanthin. V. Thermolytic Peptides of Actinoxanthin (Russian)

Bioorg.Khim. (1975)

Actinovanthin. Iv. Chymotryptic Peptides of Actinoxanthin (Russian)

Bioorg.Khim. (1975)

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Unit-cell length a length_a	30.900 Å
Unit-cell length b length_b	48.800 Å
Unit-cell length c length_c	64.100 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	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Description description	ACTINOXANTHIN
Molecular weight formula_weight	10332.1 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	721

ACTINOXANTHIN STRUCTURE AT THE ATOMIC LEVEL (RUSSIAN)

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

ACTINOXANTHIN

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (22)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Streptomyces globisporus
NCBI Class编号 ncbi_taxonomy_id	1908

fit	/app/data/saxs_computation/ac/1acx/1acx.fit
pddf	/app/data/pr_computation/ac/1acx/1acx.pr.out
profile	/app/data/saxs_computation/ac/1acx/1acx.dat