SAXSdb — 2z37

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

Chitinase

Brassica juncea

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9SQF7_BRAJU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–244； UniProt 146–389 Author chain B； PDBConstruct 1–244； UniProt 146–389 Author chain C； PDBConstruct 1–244； UniProt 146–389 Author chain D； PDBConstruct 1–244； UniProt 146–389

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	2z37
Deposition date deposition_date	2007-06-02
Structure title title	Crystal structure of Brassica juncea chitinase catalytic module (Bjchi3)
Keywords keywords	chitinase, endochitinase, family 19, conformational changes, HYDROLASE; HYDROLASE
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.

2z37__assembly_1__model_1

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

Download this curve (.dat)

2z37__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2z37__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.20 Å
Rg (electron density)	17.05 Å
Total Rg	18.05 Å
Atom count	1900
Residues	244
Excluded volume	33321 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2z37__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2z37__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2z37__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2z37__assembly_4__model_1`	monomeric （1）	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	d2z37a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.2 — Lysozyme-like
Superfamily Superfamily superfamily	d.2.1 — Lysozyme-like
Family Family family	d.2.1.1 — Family 19 glycosidase

Domain ID domain_id	d2z37b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.2 — Lysozyme-like
Superfamily Superfamily superfamily	d.2.1 — Lysozyme-like
Family Family family	d.2.1.1 — Family 19 glycosidase

Domain ID domain_id	d2z37c_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.2 — Lysozyme-like
Superfamily Superfamily superfamily	d.2.1 — Lysozyme-like
Family Family family	d.2.1.1 — Family 19 glycosidase

Domain ID domain_id	d2z37d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.2 — Lysozyme-like
Superfamily Superfamily superfamily	d.2.1 — Lysozyme-like
Family Family family	d.2.1.1 — Family 19 glycosidase

CATH v4.4 (8 domains)

Domain ID domain_id	2z37A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	530 — Lysozyme
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2z37A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	20 — Endochitinase; domain 2
Homologous superfamily homologous superfamily	10 — Endochitinase, domain 2

Domain ID domain_id	2z37B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	530 — Lysozyme
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2z37B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	20 — Endochitinase; domain 2
Homologous superfamily homologous superfamily	10 — Endochitinase, domain 2

Domain ID domain_id	2z37C01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	530 — Lysozyme
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2z37C02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	20 — Endochitinase; domain 2
Homologous superfamily homologous superfamily	10 — Endochitinase, domain 2

Domain ID domain_id	2z37D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	530 — Lysozyme
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2z37D02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	20 — Endochitinase; domain 2
Homologous superfamily homologous superfamily	10 — Endochitinase, domain 2

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Unit-cell length a length_a	51.249 Å
Unit-cell length b length_b	61.821 Å
Unit-cell length c length_c	75.359 Å
Unit-cell angle α angle_alpha	79.34 °
Unit-cell angle β angle_beta	89.52 °
Unit-cell angle γ angle_gamma	88.90 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.530 Å
Low-resolution limit resolution_low	42.230 Å
R factor r_factor	0.1880
R_work r_work	0.1850
R_free r_free	0.2220

Description description	Chitinase
Molecular weight formula_weight	27054.2 kDa
EC 编号 ec_number	3.2.1.14
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8402

Crystal structure of Brassica juncea chitinase catalytic module (Bjchi3)

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

Chitinase

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

2z37__assembly_1__model_1

2z37__assembly_1__model_1 | I(q)

2z37__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 (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 (1)

Source organism organism	Brassica juncea
NCBI taxonomy ID ncbi_taxonomy_id	3707
Host organism host_organism	Pichia pastoris

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	738

Crystal structure of Brassica juncea chitinase catalytic module (Bjchi3)

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

Chitinase

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

2z37__assembly_1__model_1

2z37__assembly_1__model_1 | I(q)

2z37__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 (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 (1)