SAXSdb — 1agx

▼

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

GLUTAMINASE-ASPARAGINASE

Acinetobacter glutaminasificans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ASPQ_ACIGL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–331； UniProt 1–331

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1agx
Deposition date deposition_date	1994-07-13
Structure title title	REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS GLUTAMINASE-ASPARAGINASE
Keywords keywords	BACTERIAL AMIDOHYDROLASE; BACTERIAL AMIDOHYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1agx__assembly_1__model_1

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

Download this curve (.dat)

1agx__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1agx__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.79 Å
Rg (electron density)	29.80 Å
Total Rg	30.69 Å
Atom count	9988
Residues	1324
Excluded volume	177970 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1agx__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1agxa_
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 (2 domains)

Domain ID domain_id	1agxA01
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	1agxA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	40 —

▶

7. Citations (7)

Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.

Acta Crystallogr.,Sect.D (1994)

PMID: 15299349 · DOI: 10.1107/S0907444994003446 PRIMARY

Structural Characterization of Pseudomonas 7A Glutaminase-Asparaginase

Biochemistry (1994)

;A Left-Handed Crossover Involved in Amidohydrolysis 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)

Preliminary Crystal Structure of Acinetobacter Glutaminasificans Glutaminase-Asparaginase

J.Biol.Chem. (1988)

;Structures of Amidohydrolases: Amino Acid Sequence of a Glutaminase-Asparaginase from Acinetobacter Glutaminasificans and Preliminary Crystallographic Data for an Asparaginase from Erwinia Chrysanthemi ;

J.Biol.Chem. (1988)

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

Acta Crystallogr.,Sect.B (1983)

Unit-cell length a length_a	96.600 Å
Unit-cell length b length_b	112.500 Å
Unit-cell length c length_c	71.200 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	I 2 2 2
Space-group number int_tables_number	23
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1710
R_work r_work	0.1710
R_free r_free	—

Description description	GLUTAMINASE-ASPARAGINASE
Molecular weight formula_weight	35523.4 kDa
EC 编号 ec_number	3.5.1.1
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2497

REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS 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

1agx__assembly_1__model_1

1agx__assembly_1__model_1 | I(q)

1agx__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (7)

Source organism organism	Acinetobacter glutaminasificans
NCBI taxonomy ID ncbi_taxonomy_id	474

REFINED CRYSTAL STRUCTURE OF ACINETOBACTER GLUTAMINASIFICANS 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

1agx__assembly_1__model_1

1agx__assembly_1__model_1 | I(q)

1agx__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (7)