SAXSdb — 1rgh

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

RIBONUCLEASE

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RNSA_STRAU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–96； UniProt 1–96 Author chain B； PDBConstruct 1–96； UniProt 1–96

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	1rgh
Deposition date deposition_date	1995-06-05
Structure title title	HYDROLASE, GUANYLORIBONUCLEASE
Keywords keywords	HYDROLASE (GUANYLORIBONUCLEASE); HYDROLASE (GUANYLORIBONUCLEASE)
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1rgh__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1rgh__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1rgh__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	21.55 Å
Rg (electron density)	21.00 Å
Total Rg	21.75 Å
Atom count	2882
Residues	192
Excluded volume	26178 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1rgh__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1rgha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.1 — Microbial ribonucleases
Superfamily Superfamily superfamily	d.1.1 — Microbial ribonucleases
Family Family family	d.1.1.2 — Bacterial ribonucleases

Domain ID domain_id	d1rghb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.1 — Microbial ribonucleases
Superfamily Superfamily superfamily	d.1.1 — Microbial ribonucleases
Family Family family	d.1.1.2 — Bacterial ribonucleases

CATH v4.4 (2 domains)

Domain ID domain_id	1rghA00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	30 — Microbial ribonucleases

Domain ID domain_id	1rghB00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily	30 — Microbial ribonucleases

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7. Citations (8)

Ribonuclease from Streptomyces aureofaciens at atomic resolution.

Acta Crystallogr.,Sect.D (1996)

PMID: 15299705 · DOI: 10.1107/S0907444995007669 PRIMARY

;Complex of Ribonuclease from Streptomyces Aureofaciens with 2'-Gmp at 1.7A Resolution ;

Acta Crystallogr.,Sect.D (1993)

Complex of Ribonuclease Sa with a Cyclic Nucleotide and a Proposed Model for the Reaction Intermediate

Eur.J.Biochem. (1993)

;Determination and Restrained Least-Squares Refinement of the Structures of Ribonuclease Sa and its Complex with 3'-Guanylic Acid at 1.8 A Resolution ;

Acta Crystallogr.,Sect.B (1991)

Comparison of Active Sites of Some Microbial Ribonucleases: Structural Basis for Guanylic Specificity

Trends Biochem.Sci. (1990)

Amino Acid Sequence Determination of Guanyl-Specific Ribonuclease Sa from Streptomyces Aureofaciens

FEBS Lett. (1986)

Exocellular Ribonuclease from Streptomyces Aureofaciens. I. Isolation and Purification

Biochim.Biophys.Acta (1971)

Exocellular Ribonuclease from Streptomyces Aureofaciens. II. Properties and Specificity

Biochim.Biophys.Acta (1971)

Unit-cell length a length_a	64.820 Å
Unit-cell length b length_b	78.560 Å
Unit-cell length c length_c	39.050 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	8

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

Resolution resolution	1.200 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Description description	RIBONUCLEASE
Molecular weight formula_weight	10582.5 kDa
EC 编号 ec_number	3.1.27.3
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3185

HYDROLASE, GUANYLORIBONUCLEASE

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

RIBONUCLEASE

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1rgh__assembly_1__model_1

1rgh__assembly_1__model_1 | I(q)

1rgh__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (8)

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	292

HYDROLASE, GUANYLORIBONUCLEASE

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

RIBONUCLEASE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1rgh__assembly_1__model_1

1rgh__assembly_1__model_1 | I(q)

1rgh__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (8)