SAXSdb — 2bxy

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

MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE

DEINOCOCCUS RADIODURANS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Other combination	Monomer	Protein 1 其他Polymer 2	alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose × 2 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 alpha-D-glucopyranose × 2 BETA-MERCAPTOETHANOL × 1 MAGNESIUM ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9RX51_DEIRA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–430； UniProt 1–430 Author chain A； PDBConstruct 433–602； UniProt 431–600

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	2bxy
Deposition date deposition_date	2005-07-28
Structure title title	Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection
Keywords keywords	DATA COLLECTION, RADIATION DAMAGE, DOSE-RATE, SYNCHROTRON RADIATION, 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.

2bxy__assembly_1__model_1

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

Download this curve (.dat)

2bxy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2bxy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.67 Å
Rg (electron density)	24.71 Å
Total Rg	25.57 Å
Atom count	4684
Residues	572
Excluded volume	82233 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2bxy__assembly_1__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 (7)

Entity 1 Entity 1 polymer

Description description	MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE
Molecular weight formula_weight	67623.8 kDa
EC 编号 ec_number	3.2.1.1
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	5804

MTQTQPVTPTPPASFQTQHDPRTRLGATPLPGGAGTRFRLWTSTARTVAVRVNGTEHVMTSLGGGIYELELPVGPGARYLFVLDGVPTPDPYARFLPDGVHGEAEVVDFGTFDWTDADWHGIKLADCVFYEVHVGTFTPEGTYRAAAEKLPYLKELGVTAIQVMPLAAFDGQRGWGYDGAAFYAPYAPYGRPEDLMALVDAAHRLGLGVFLDVVYNHFGPSGNYLSSYAPSYFTDRFSSAWGMGLDYAEPHMRRYVTGNARMWLRDYHFDGLRLDATPYMTDDSETHILTELAQEIHELGGTHLLLAEDHRNLPDLVTVNHLDGIWTDDFHHETRVTLTGEQEGYYAGYRGGAEALAYTIRRGWRYEGQFWAVKGEEHERGHPSDALEAPNFVYCIQNHDQIGNRPLGERLHQSDGVTLHEYRGAAALLLTLPMTPLLFQGQEWAASTPFQFFSDHAGELGQAVSEGRKKEFGGFSGFSGEDVPDPQAEQTFLNSKLNWAEREGGEHARTLRLYRDLLRLRREDPVLHNRQRENLTTGHDGDVLWVRTVTGAGERVLLWNLGQDTRAVAEVKLPFTVPRRLLLHTEGREDLTLGAGEAVLVG

Source Source

Source organism organism	DEINOCOCCUS RADIODURANS
NCBI taxonomy ID ncbi_taxonomy_id	243230
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 branched

Description description	alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Molecular weight formula_weight	122.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	alpha-D-glucopyranose
Molecular weight formula_weight	180.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	BETA-MERCAPTOETHANOL
Molecular weight formula_weight	78.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	856

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2bxya1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.2 — E-set domains of sugar-utilizing enzymes

Domain ID domain_id	d2bxya2
Class class	b — All beta proteins
Fold Fold fold	b.71 — Glycosyl hydrolase domain
Superfamily Superfamily superfamily	b.71.1 — Glycosyl hydrolase domain
Family Family family	b.71.1.1 — alpha-Amylases, C-terminal beta-sheet domain

Domain ID domain_id	d2bxya3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.1 — Amylase, catalytic domain

CATH v4.4 (4 domains)

Domain ID domain_id	2bxyA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	2bxyA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	2bxyA03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	760 — E-set domains of sugar-utilizing enzymes

Domain ID domain_id	2bxyA04
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1180 — Golgi alpha-mannosidase II

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Unit-cell length a length_a	59.418 Å
Unit-cell length b length_b	66.529 Å
Unit-cell length c length_c	152.522 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	1.750 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1490
R_work r_work	0.1470
R_free r_free	0.1880

Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

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

MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE

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

2bxy__assembly_1__model_1

2bxy__assembly_1__model_1 | I(q)

2bxy__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

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

MALTOOLIGOSYLTREHALOSE TREHALOHYDROLASE

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

2bxy__assembly_1__model_1

2bxy__assembly_1__model_1 | I(q)

2bxy__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (1)