SAXSdb — 3o5t

▼

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

Dinitrogenase reductase activacting glicohydrolase

Azospirillum brasilense

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	PII-like protein Pz × 3 （P70731） MAGNESIUM ION × 6 ADENOSINE-5'-DIPHOSPHATE × 3 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A7XNI2_AZOBR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–297； UniProt 1–297

PII-like protein Pz

Azospirillum brasilense

UniProt P70731

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 6	Dinitrogenase reductase activacting glicohydrolase × 3 （A7XNI2） MAGNESIUM ION × 6 ADENOSINE-5'-DIPHOSPHATE × 3 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P70731_AZOBR
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–112； UniProt 1–112

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	3o5t
Deposition date deposition_date	2010-07-28
Structure title title	Structure of DraG-GlnZ complex with ADP
Keywords keywords	ADP binding, HYDROLASE-TRANSCRIPTION complex; HYDROLASE/TRANSCRIPTION
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.

3o5t__assembly_1__model_1

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

Download this curve (.dat)

3o5t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3o5t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	40.20 Å
Rg (electron density)	39.91 Å
Total Rg	39.96 Å
Atom count	9168
Residues	1185
Excluded volume	162440 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3o5t__assembly_1__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Dinitrogenase reductase activacting glicohydrolase
Molecular weight formula_weight	32442.8 kDa
EC 编号 ec_number	3.2.2.24
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3449

MTDHSIRSRALGAYLGLACGDALGATVEFLTKGEIAHQYGVHKHIKGGGWLKLPAGQVTDDTEMSIHLGRAILAAPEWDARRAAEEFAVWLKGVPVDVGDTTRRGIRRFIMHGTLSEPESEYHAGNGAAMRNLPVALATLGDDAAFERWTVEQAHITHCNAMSDAATLTLGHMVRRLVLGGDVRDVRDESNKLIAKHRQFKFQPYRGLATAYIVDTMQTVMHYYFQTDSVESCVVETVNQGGDADTTGAIAGMLAGATYGVETIPPRWLRKLDRDVYNEICAQVDGLLARAPALKQG

Source Source

Source organism organism	Azospirillum brasilense
NCBI taxonomy ID ncbi_taxonomy_id	192
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PII-like protein Pz
Molecular weight formula_weight	12287.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MKLVMAIIKPFKLDEVREALTSLGIQGLTVSEVKGFGRQKGQTEIYRGAEYSVSFLPKVKVEVAVSDDQYEQVVEAIQKAANTGRIGDGKIFVLDIAQAVRIRTGETNTEAL

Source Source

Source organism organism	Azospirillum brasilense
NCBI taxonomy ID ncbi_taxonomy_id	192
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	393

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3o5ta_
Class class	a — All alpha proteins
Fold Fold fold	a.209 — ADP-ribosylglycohydrolase
Superfamily Superfamily superfamily	a.209.1 — ADP-ribosylglycohydrolase
Family Family family	a.209.1.0 — automated matches

Domain ID domain_id	d3o5tb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.5 — GlnB-like
Family Family family	d.58.5.1 — Prokaryotic signal transducing protein

CATH v4.4 (2 domains)

Domain ID domain_id	3o5tA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	4080 — ADP-ribosylglycohydrolase fold
Homologous superfamily homologous superfamily	10 — ADP-ribosylation/Crystallin J1

Domain ID domain_id	3o5tB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	120 —

▶

Unit-cell length a length_a	115.654 Å
Unit-cell length b length_b	115.654 Å
Unit-cell length c length_c	105.626 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	9

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.090 Å
Low-resolution limit resolution_low	70.000 Å
R factor r_factor	0.1532
R_work r_work	0.1511
R_free r_free	0.1911

Structure of DraG-GlnZ complex with ADP

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

Dinitrogenase reductase activacting glicohydrolase

State in the Current Structure

Other States of the Same Protein in the Database

PII-like protein Pz

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

3o5t__assembly_1__model_1

3o5t__assembly_1__model_1 | I(q)

3o5t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Structure of DraG-GlnZ complex with ADP

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

Dinitrogenase reductase activacting glicohydrolase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PII-like protein Pz

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

3o5t__assembly_1__model_1

3o5t__assembly_1__model_1 | I(q)

3o5t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)