SAXSdb — 3pga

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

GLUTAMINASE-ASPARAGINASE

Pseudomonas sp. 7A

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ASPQ_PSES7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 8–337； UniProt 8–337 Author chain 2； PDBConstruct 8–337； UniProt 8–337 Author chain 3； PDBConstruct 8–337； UniProt 8–337 Author chain 4； PDBConstruct 8–337； UniProt 8–337

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	3pga
Deposition date deposition_date	1994-07-19
Structure title title	STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE
Keywords keywords	BACTERIAL AMIDOHYDROLASE; BACTERIAL AMIDOHYDROLASE
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.

3pga__assembly_1__model_1

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

Download this curve (.dat)

3pga__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3pga__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.75 Å
Rg (electron density)	29.65 Å
Total Rg	30.59 Å
Atom count	9424
Residues	1238
Excluded volume	167580 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3pga__assembly_1__model_1`	tetrameric （4）	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) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3pga1_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.88 — Glutaminase/Asparaginase
Superfamily Superfamily superfamily	c.88.1 — Glutaminase/Asparaginase
Family Family family	c.88.1.1 — Glutaminase/Asparaginase

Domain ID domain_id	d3pga2_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.88 — Glutaminase/Asparaginase
Superfamily Superfamily superfamily	c.88.1 — Glutaminase/Asparaginase
Family Family family	c.88.1.1 — Glutaminase/Asparaginase

Domain ID domain_id	d3pga3_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.88 — Glutaminase/Asparaginase
Superfamily Superfamily superfamily	c.88.1 — Glutaminase/Asparaginase
Family Family family	c.88.1.1 — Glutaminase/Asparaginase

Domain ID domain_id	d3pga4_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.88 — Glutaminase/Asparaginase
Superfamily Superfamily superfamily	c.88.1 — Glutaminase/Asparaginase
Family Family family	c.88.1.1 — Glutaminase/Asparaginase

CATH v4.4 (8 domains)

Domain ID domain_id	3pga101
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1170 — L-asparaginase, N-terminal domain

Domain ID domain_id	3pga102
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	3pga201
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1170 — L-asparaginase, N-terminal domain

Domain ID domain_id	3pga202
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	3pga301
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1170 — L-asparaginase, N-terminal domain

Domain ID domain_id	3pga302
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	40 —

Domain ID domain_id	3pga401
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1170 — L-asparaginase, N-terminal domain

Domain ID domain_id	3pga402
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	40 —

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7. Citations (7)

Structural characterization of Pseudomonas 7A glutaminase-asparaginase.

Biochemistry (1994)

PMID: 8068664 · DOI: 10.1021/bi00200a005 PRIMARY

;A Left-Handed Crossover Involved in Amidohydrolase Catalysis: Crystal Structure of Erwinia Chrysanthemi L-Asparaginase with Bound L-Aspartate ;

FEBS Lett. (1993)

Crystal Structure of E. Coli L-Asparaginase, an Enzyme Used in Cancer Therapy

Proc.Natl.Acad.Sci.USA (1993)

The Molecular Symmetry of Glutaminase-Asparaginases: Rotation Function Studies of the Pseudomonas 7A and Acinetobacter Enzymes

Acta Crystallogr.,Sect.B (1983)

Amino Acid Sequence of the Diazooxonorleucine Binding Site of Acinetobacter and Pseudomonas 7A Glutaminase-Asparaginase Enzymes

Biochemistry (1978)

Characterization of Crystals of L-Glutaminase-Asparaginase from Acinetobacter Glutaminasificans and Pseudomonas 7A

J.Mol.Biol. (1977)

Refined Crystal Structure of Acinetobacter Glutaminasificans Glutaminase-Asparaginase

To be Published

Unit-cell length a length_a	118.260 Å
Unit-cell length b length_b	130.750 Å
Unit-cell length c length_c	85.090 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	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	10.000 Å
R factor r_factor	0.1650
R_work r_work	0.1650
R_free r_free	—

Description description	GLUTAMINASE-ASPARAGINASE
Molecular weight formula_weight	35978.7 kDa
EC 编号 ec_number	3.5.1.1
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,3,4
Atom count atom_count	10854

STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE

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

GLUTAMINASE-ASPARAGINASE

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

3pga__assembly_1__model_1

3pga__assembly_1__model_1 | I(q)

3pga__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) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (7)

Source organism organism	Pseudomonas sp. 7A
NCBI taxonomy ID ncbi_taxonomy_id	65406

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	418

STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE

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

GLUTAMINASE-ASPARAGINASE

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

3pga__assembly_1__model_1

3pga__assembly_1__model_1 | I(q)

3pga__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) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (7)