SAXSdb — 9izo

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

Maltodextrin glucosidase

Klebsiella grimontii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	;(2~{S},3~{R},4~{S},5~{R},6~{R})-5-[[(1~{S},4~{R},5~{S},6~{S})-3-(hydroxymethyl)-4,5,6-tris(oxidanyl)cyclohex-2-en-1-yl]amino]-6-methyl-oxane-2,3,4-triol ; × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A7H4P971_9ENTR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–605； UniProt 1–605

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	9izo
Deposition date deposition_date	2024-08-01
Structure title title	Apg mutant enzyme D336A of acarbose hydrolase from human gut flora K. grimontii TD1, complex with acarviosine
Keywords keywords	Hydrolase, Complex; 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.

9izo__assembly_1__model_1

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

Download this curve (.dat)

9izo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9izo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.20 Å
Rg (electron density)	31.29 Å
Total Rg	31.98 Å
Atom count	9484
Residues	1172
Excluded volume	166810 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9izo__assembly_1__model_1`	dimeric （2）	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 (3)

Entity 1 Entity 1 polymer

Description description	Maltodextrin glucosidase
Molecular weight formula_weight	69064.6 kDa
EC 编号 ec_number	3.2.1.135,3.2.1.20
Mutation mutation	D336A
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	5030

MLKAWHLPVAPFIKEQQERLMITLWLSGDDLPPRVTLRAEEDNEELSLPMHRLRQAPHPGVVAWRGEINLVNGQPRRRYSFKLLWADRQLWFTPQEFNRFPPARLEQFAVDLPDSGPQWVADQVFYQIFPDRFARSQSREAEQDATYYHHAAGHDIVRKAWDEPLTAEAGGSTFYGGDLDGISEKLPYLKQLGVTALYLNPVFVAPSVHKYDTEDYRRVDPQFGGDAALLRLRHNTQKEGMRLILDGVFNHSGDSHAWFDRHQRGSGGACHNADSPWRDWYNFSPEGVAHDWLGYASLPKLDYRSSTLIDEIYGGEDSVVRHWLKAPWSMDGWRLAVVHMLGEGGGARNNLRHIAGITQAAKLERPDAFVFGEHFGDARQWLQADVEDSAMNYRGFTFPLWGFLANTDISYDPQKIDAQTCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKSLLGKDVARLPLAVVWLFSWPGVPCIYYGDEVGVDGNNDPFCRKPFPWDPALQDGDLLDLYKRMSKLRKAHQALRYGGCQVIYAEDNVVVFVRVYKQQRVLVAINRGEACEVVIEDSPLLDVNGWQLKEGAGALHDGVLTLPAISASVWFSR

Source Source

Source organism organism	Klebsiella grimontii
NCBI taxonomy ID ncbi_taxonomy_id	2058152
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	;(2~{S},3~{R},4~{S},5~{R},6~{R})-5-[[(1~{S},4~{R},5~{S},6~{S})-3-(hydroxymethyl)-4,5,6-tris(oxidanyl)cyclohex-2-en-1-yl]amino]-6-methyl-oxane-2,3,4-triol ;
Molecular weight formula_weight	321.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	288

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Unit-cell length a length_a	75.510 Å
Unit-cell length b length_b	75.510 Å
Unit-cell length c length_c	399.409 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 65 2 2
Space-group number int_tables_number	179
Crystal system crystal_system	hexagonal

Resolution resolution	2.130 Å
Low-resolution limit resolution_low	46.650 Å
R factor r_factor	0.2106
R_work r_work	0.2086
R_free r_free	0.2479

Apg mutant enzyme D336A of acarbose hydrolase from human gut flora K. grimontii TD1, complex with acarviosine

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

Maltodextrin glucosidase

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

9izo__assembly_1__model_1

9izo__assembly_1__model_1 | I(q)

9izo__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)

Apg mutant enzyme D336A of acarbose hydrolase from human gut flora K. grimontii TD1, complex with acarviosine

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

Maltodextrin glucosidase

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

9izo__assembly_1__model_1

9izo__assembly_1__model_1 | I(q)

9izo__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)