SAXSdb — 2vwg

▼

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

GLUCOSE DEHYDROGENASE

HALOFERAX MEDITERRANEI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 D-glucono-1,5-lactone × 2 ZINC ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q977U7_HALME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–357； UniProt 1–357

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	2vwg
Deposition date deposition_date	2008-06-24
Structure title title	Haloferax mediterranei glucose dehydrogenase in complex with NADP, Zn and gluconolactone.
Keywords keywords	OXIDOREDUCTASE, ZINC DEPENDENT MEDIUM CHAIN ALCOHOL DEHYDROGENASE FAMILY, GLUCOSE DEHYDROGENASE, ALCOHOL DEHYDROGENASE; OXIDOREDUCTASE
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.

2vwg__assembly_1__model_1

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

Download this curve (.dat)

2vwg__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2vwg__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.36 Å
Rg (electron density)	28.87 Å
Total Rg	29.51 Å
Atom count	5662
Residues	714
Excluded volume	99581 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2vwg__assembly_1__model_1`	dimeric （2）	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	GLUCOSE DEHYDROGENASE
Molecular weight formula_weight	39282.7 kDa
EC 编号 ec_number	1.1.1.47
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	2974

MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVDGTDHEVIAGGHGGFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFERDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIEPISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYENLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEATGFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVGSVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKTAIEFSTV

Source Source

Source organism organism	HALOFERAX MEDITERRANEI
NCBI taxonomy ID ncbi_taxonomy_id	2252
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Molecular weight formula_weight	743.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	D-glucono-1,5-lactone
Molecular weight formula_weight	178.1 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 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	143

▼

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2vwgA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	180 — Quinone Oxidoreductase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Medium-chain alcohol dehydrogenases, catalytic domain

Domain ID domain_id	2vwgA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

▶

Unit-cell length a length_a	61.647 Å
Unit-cell length b length_b	112.205 Å
Unit-cell length c length_c	150.597 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	2.000 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.1360
R_work r_work	0.1350
R_free r_free	0.1590

Haloferax mediterranei glucose dehydrogenase in complex with NADP, Zn and gluconolactone.

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

GLUCOSE DEHYDROGENASE

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

2vwg__assembly_1__model_1

2vwg__assembly_1__model_1 | I(q)

2vwg__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)

Haloferax mediterranei glucose dehydrogenase in complex with NADP, Zn and gluconolactone.

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

GLUCOSE DEHYDROGENASE

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

2vwg__assembly_1__model_1

2vwg__assembly_1__model_1 | I(q)

2vwg__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)