SAXSdb — 9maq

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

Alpha-1,4 glucan phosphorylase

Dorea longicatena DSM 13814

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A174FL20_9FIRM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–753； UniProt 1–752 Author chain B； PDBConstruct 2–753； UniProt 1–752

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	9maq
Deposition date deposition_date	2025-03-14
Structure title title	Glycogen phosphorylase from D. longicatena
Keywords keywords	glycogen metabolism, cryo-EM, gut bacteria, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
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.

9maq__assembly_1__model_1

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

Download this curve (.dat)

9maq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9maq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	42.25 Å
Rg (electron density)	41.65 Å
Total Rg	42.01 Å
Atom count	12128
Residues	1504
Excluded volume	216910 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9maq__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 (1)

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Unit-cell length a length_a	103.969 Å
Unit-cell length b length_b	122.851 Å
Unit-cell length c length_c	136.004 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	8

Space group space_group	P 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	3.800 Å
Low-resolution limit resolution_low	48.560 Å
R factor r_factor	0.2046
R_work r_work	0.2014
R_free r_free	0.2655

Description description	Alpha-1,4 glucan phosphorylase
Molecular weight formula_weight	86238.1 kDa
EC 编号 ec_number	2.4.1.1
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	12128

Glycogen phosphorylase from D. longicatena

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

Alpha-1,4 glucan phosphorylase

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

9maq__assembly_1__model_1

9maq__assembly_1__model_1 | I(q)

9maq__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)

Source organism organism	Dorea longicatena DSM 13814
NCBI taxonomy ID ncbi_taxonomy_id	411462
Host organism host_organism	Escherichia coli BL21(DE3)

Glycogen phosphorylase from D. longicatena

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

Alpha-1,4 glucan phosphorylase

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

9maq__assembly_1__model_1

9maq__assembly_1__model_1 | I(q)

9maq__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

7. Citations (1)