SAXSdb — 3ut0

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

Exo-1,3/1,4-beta-glucanase

Pseudoalteromonas sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 SODIUM ION × 1 SULFATE ION × 5 1,2-ETHANEDIOL × 3 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 SODIUM ION × 1 SULFATE ION × 5 1,2-ETHANEDIOL × 2 water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 SODIUM ION × 1 SULFATE ION × 5 1,2-ETHANEDIOL × 2 water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	CALCIUM ION × 1 SODIUM ION × 1 SULFATE ION × 3 1,2-ETHANEDIOL × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0QJA3_9GAMM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–814； UniProt 28–840 Author chain B； PDBConstruct 2–814； UniProt 28–840 Author chain C； PDBConstruct 2–814； UniProt 28–840 Author chain D； PDBConstruct 2–814； UniProt 28–840

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	3ut0
Deposition date deposition_date	2011-11-24
Structure title title	Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1
Keywords keywords	(ALPHA/BETA)8 BARREL, (ALPHA/BETA)6 SHEET, BETA-SANDWICH, 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.

3ut0__assembly_1__model_1

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

Download this curve (.dat)

3ut0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3ut0__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)	28.56 Å
Total Rg	29.44 Å
Atom count	6267
Residues	804
Excluded volume	110800 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3ut0__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3ut0__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3ut0__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3ut0__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 (6)

Entity 1 Entity 1 polymer

Description description	Exo-1,3/1,4-beta-glucanase
Molecular weight formula_weight	90621.6 kDa
EC 编号 ec_number	3.2.1.-
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	25742

MAEHEQVNWPYVNTKLKRDPAVEAQIEKLLAKMTIEQKVAQMIQPEIGYLTVEQMRKYGFGSYLNGGNTAPYGNKRADQATWLKYADEMYLAAMDSTLDGIAIPTVWGTDAMHGHSNVYGATLFPHNIGLGAARDTDLIKRIGQATAKEVAATGIEWSFAPTVAVVRDDRWGRTYESYSEDPDLVKRYAGEMVTGIQGDVGADFLKGSNRIATAKHFVGDGGTERGVDRGNTLIDEKGLRDIHSAGYFSAINQGVQSVMASFNSWNGKRVHGDKHLLTDVLKNQLGFDGFVVSDWNAHKFVEGCDLEQCAQAINAGVDVIMVPEHFEAFYHNTVKQVKAGVIAESRINDAVRRFLRAKIRWGVFTKSKPSARPESQHPQWLGAAEHRTLAREAVRKSLVLLKNNESILPIKASSRILVAGKGANAINMQAGGWSVSWQGTDNTNSDFPNATSIFSGLQSQVTKAGGKITLSESGEYTSKPDVAIVVIGEEPYAEWFGDIELLEFQHETKHALALLKQLKADNIPVVTVFLSGRPLWVNKELNASDAFVAAWLPGSEGEGVADVLLTNKQGKTQFDFTGKLSFSWPKYDDQFTLNLNDADYDPLFAYGYGLTYQDNINVPVLSEKTSPKKTVNSDSHPLFVRSLAKNMTWQLADTSTQKVLASGASATSGDKQSLLMQSVNLSYQEDGRGFNWRAQAALSLSYLEPTPLDSKFSTGYLELKMRIDKAPEQGANLQVMCSESNCLRDIDFSSFSQLMADKSWHTLAIPLHCDDSDQAEQPITDALRITSQNLSLAIADVALTIKPSDDSISLTCAKLEHHHHHH

Source Source

Source organism organism	Pseudoalteromonas sp.
NCBI taxonomy ID ncbi_taxonomy_id	368972
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 5 Entity 5 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	828

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	3ut0A01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	300 — Glycoside hydrolase, family 3, N-terminal domain

Domain ID domain_id	3ut0A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1700 — Glycoside hydrolase family 3 C-terminal domain

Domain ID domain_id	3ut0A03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

Domain ID domain_id	3ut0B01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	300 — Glycoside hydrolase, family 3, N-terminal domain

Domain ID domain_id	3ut0B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1700 — Glycoside hydrolase family 3 C-terminal domain

Domain ID domain_id	3ut0B03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

Domain ID domain_id	3ut0C01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	300 — Glycoside hydrolase, family 3, N-terminal domain

Domain ID domain_id	3ut0C02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1700 — Glycoside hydrolase family 3 C-terminal domain

Domain ID domain_id	3ut0C03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

Domain ID domain_id	3ut0D01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	300 — Glycoside hydrolase, family 3, N-terminal domain

Domain ID domain_id	3ut0D02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1700 — Glycoside hydrolase family 3 C-terminal domain

Domain ID domain_id	3ut0D03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	430 — Galactose-binding lectin

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Unit-cell length a length_a	84.908 Å
Unit-cell length b length_b	257.821 Å
Unit-cell length c length_c	85.605 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	115.47 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	38.328 Å
R factor r_factor	0.2252
R_work r_work	0.2227
R_free r_free	0.2701

Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1

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

Exo-1,3/1,4-beta-glucanase

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

3ut0__assembly_1__model_1

3ut0__assembly_1__model_1 | I(q)

3ut0__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)

Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1

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

Exo-1,3/1,4-beta-glucanase

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

3ut0__assembly_1__model_1

3ut0__assembly_1__model_1 | I(q)

3ut0__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (1)