SAXSdb — 2sga

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

PROTEINASE A

Streptomyces griseus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PRTA_STRGR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–181； UniProt 117–297

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	2sga
Deposition date deposition_date	1983-01-21
Structure title title	ELECTRON DENSITY CALCULATIONS AS AN EXTENSION OF PROTEIN STRUCTURE REFINEMENT. STREPTOMYCES GRISEUS PROTEASE AT 1.5 ANGSTROMS RESOLUTION
Keywords keywords	HYDROLASE (SERINE PROTEINASE); HYDROLASE (SERINE PROTEINASE)
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.

2sga__assembly_1__model_1

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

Download this curve (.dat)

2sga__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2sga__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	15.49 Å
Rg (electron density)	14.35 Å
Total Rg	15.42 Å
Atom count	1259
Residues	181
Excluded volume	21865 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2sga__assembly_1__model_1`	monomeric （1）	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 (2)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2sgaa_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.1 — Prokaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id	2sgaA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

Domain ID domain_id	2sgaA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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7. Citations (9)

Electron density calculations as an extension of protein structure refinement. Streptomyces griseus protease A at 1.5 A resolution.

J.Mol.Biol. (1985)

PMID: 3892015 · DOI: 10.1016/0022-2836(85)90241-4 PRIMARY

;Structures of Product and Inhibitor Complexes of Streptomyces Griseus Protease a at 1.8 Angstroms Resolution. A Model for Serine Protease Catalysis ;

J.Mol.Biol. (1980)

;Structure of the Complex Formed between the Bacterial-Produced Inhibitor Chymostatin and the Serine Enzyme Streptomyces Griseus Protease A ;

J.Mol.Biol. (1980)

Protein Structure Refinement. Streptomyces Griseus Serine Protease a at 1.8 Angstroms Resolution

J.Mol.Biol. (1979)

;Crystallographic and Kinetic Investigations of the Covalent Complex Formed by a Specific Tetrapeptide Aldehyde and the Serine Protease from Streptomyces Griseus ;

Proc.Natl.Acad.Sci.USA (1979)

;Molecular Structure of Crystalline Streptomyces Griseus Protease a at 2.8 Angstroms Resolution. II. Molecular Conformation, Comparison with Alpha-Chymotrypsin and Active-Site Geometry ;

J.Mol.Biol. (1978)

;Molecular Structure of Crystalline Streptomyces Griseus Protease a at 2.8 Angstroms Resolution. I. Crystallization, Data Collection and Structural Analysis ;

J.Mol.Biol. (1978)

Amino Acid Sequence Alignment of Bacterial and Mammalian Pancreatic Serine Proteases Based on Topological Equivalences

Can.J.Biochem. (1978)

Tertiary Structural Differences between Microbial Serine Proteases and Pancreatic Serine Enzymes

Nature (1975)

Unit-cell length a length_a	55.120 Å
Unit-cell length b length_b	55.120 Å
Unit-cell length c length_c	54.810 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 42
Space-group number int_tables_number	77
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	12.000 Å
R factor r_factor	—
R_work r_work	0.1260
R_free r_free	—

Description description	PROTEINASE A
Molecular weight formula_weight	18016.6 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	1479

ELECTRON DENSITY CALCULATIONS AS AN EXTENSION OF PROTEIN STRUCTURE REFINEMENT. STREPTOMYCES GRISEUS PROTEASE AT 1.5 ANGSTROMS RESOLUTION

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

PROTEINASE A

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

2sga__assembly_1__model_1

2sga__assembly_1__model_1 | I(q)

2sga__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (9)

Source organism organism	Streptomyces griseus
NCBI taxonomy ID ncbi_taxonomy_id	1911

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	220

ELECTRON DENSITY CALCULATIONS AS AN EXTENSION OF PROTEIN STRUCTURE REFINEMENT. STREPTOMYCES GRISEUS PROTEASE AT 1.5 ANGSTROMS RESOLUTION

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

PROTEINASE A

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

2sga__assembly_1__model_1

2sga__assembly_1__model_1 | I(q)

2sga__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (9)