SAXSdb — 2i0z

▼

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

NAD(FAD)-utilizing dehydrogenases

Bacillus cereus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	CHLORIDE ION × 1 FLAVIN-ADENINE DINUCLEOTIDE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q816V9_BACCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 25–447； UniProt 1–423

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	2i0z
Deposition date deposition_date	2006-08-11
Structure title title	Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases
Keywords keywords	;Structural Genomics, NAD(FAD)-utilizing dehydrogenases, PSI-2, Protein Structure Initiative, Midwest Center for Structural Genomics, MCSG, OXIDOREDUCTASE ;; 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.

2i0z__assembly_1__model_1

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

Download this curve (.dat)

2i0z__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2i0z__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.34 Å
Rg (electron density)	26.09 Å
Total Rg	26.65 Å
Atom count	3246
Residues	416
Excluded volume	57954 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2i0z__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	NAD(FAD)-utilizing dehydrogenases
Molecular weight formula_weight	49012.8 kDa
Mutation mutation	P99H
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	3716

MHHHHHHSSGVDLGTENLYFQSNAMHYDVIVIGGGPSGLMAAIGAAEEGANVLLLDKGNKLGRKLAISGGGRCNVTNRLPLDEIVKHIPGNGRFLYSAFSIFNNEDIITFFENLGVKLKEEDHGRMFPVSNKAQSVVDALLTRLKDLGVKIRTNTPVETIEYENGQTKAVILQTGEVLETNHVVIAVGGKSVPQTGSTGDGYAWAEKAGHTITELFPTEVPILSNEPFIRDRSLQGLALRDINLSVLNPKGKAIISHKMDMLFTHFGLSGPAALRCSQFVVKALKKFKTNTIQMSIDALPEENSEQLFQRMLKQMKEDPKKGIKNVLKGYVPERYFLFLLEKNEIDGSEQAGQVSHEKIRALVKDFKEFTVNVNGTQSIEKAFVTGGGVSVKEINPKEMSSKFTNGLYFCGEVLDIHGYTGGYNITSALVTGRIAGTTAGENAKMQY

Source Source

Source organism organism	Bacillus cereus
NCBI taxonomy ID ncbi_taxonomy_id	1396
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	373

▼

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2i0za1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.8 — HI0933 N-terminal domain-like

Domain ID domain_id	d2i0za2
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.74 — HI0933 insert domain-like
Superfamily Superfamily superfamily	e.74.1 — HI0933 insert domain-like
Family Family family	e.74.1.1 — HI0933 insert domain-like

CATH v4.4 (1 domains)

Domain ID domain_id	2i0zA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

▶

Unit-cell length a length_a	46.716 Å
Unit-cell length b length_b	92.366 Å
Unit-cell length c length_c	97.504 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.840 Å
Low-resolution limit resolution_low	24.860 Å
R factor r_factor	0.1978
R_work r_work	0.1952
R_free r_free	0.2479

Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases

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

NAD(FAD)-utilizing dehydrogenases

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

2i0z__assembly_1__model_1

2i0z__assembly_1__model_1 | I(q)

2i0z__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases

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

NAD(FAD)-utilizing dehydrogenases

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

2i0z__assembly_1__model_1

2i0z__assembly_1__model_1 | I(q)

2i0z__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)