SAXSdb — 7ctm

▼

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

Alpha-glucosidase, putative

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 2 beta-D-glucopyranuronic acid × 2 ISOPROPYL ALCOHOL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9WZL1_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–483； UniProt 1–471

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	7ctm
Deposition date deposition_date	2020-08-19
Structure title title	Crystal structure of Thermotoga maritima alpha-glucuronidase (TM0752) in complex with NADH and D-glucuronic acid
Keywords keywords	;Glycosyl hydrolase family 4, NAD(P)-binding Rossmann-fold domain, LDH C-terminal domain-like, hydrolase activity, alpha-glucuronidase, HYDROLASE ;; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

7ctm__assembly_1__model_1

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

Download this curve (.dat)

7ctm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7ctm__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.22 Å
Rg (electron density)	31.67 Å
Total Rg	32.30 Å
Atom count	15110
Residues	936
Excluded volume	137030 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7ctm__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Alpha-glucosidase, putative
Molecular weight formula_weight	56927.9 kDa
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	8018

MGSDKIHHHHHHMKISIIGAGSVRFALQLVGDIAQTEELSREDTHIYMMDVHERRLNASYILARKYVEELNSPVKIVKTSSLDEAIDGADFIINTAYPYDPRYHDSGSQRWDEVTKVGEKHGYYRGIDSQELNMVSTYTYVLSSYPDMKLALEIAEKMKKMAPKAYLMQTANPVFEITQAVRRWTGANIVGFCHGVAGVYEVFEKLDLDPEEVDWQVAGVNHGIWLNRFRYRGEDAYPLLDEWIEKKLPEWEPKNPWDTQMSPAAMDMYKFYGMLPIGDTVRNGSWKYHYNLETKKKWFGKFGGIDNEVERPKFHEQLRRARERLIKLAEEVQQNPGMKLTEEHPEIFPKGKLSGEQHIPFINAIANNKRVRLFLNVENQGTLKDFPDDVVMELPVWVDCCGIHREKVEPDLTHRIKIFYLWPRILRMEWNLEAYISRDRKVLEEILIRDPRTKSYEQIVQVLDEIFNLPFNEELRRYYKEKL

Source Source

Source organism organism	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
Molecular weight formula_weight	665.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	beta-D-glucopyranuronic acid
Molecular weight formula_weight	194.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	ISOPROPYL ALCOHOL
Molecular weight formula_weight	60.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	429

▶

Unit-cell length a length_a	74.150 Å
Unit-cell length b length_b	80.590 Å
Unit-cell length c length_c	88.630 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	102.87 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.850 Å
Low-resolution limit resolution_low	36.798 Å
R factor r_factor	0.1545
R_work r_work	0.1523
R_free r_free	0.1964

Crystal structure of Thermotoga maritima alpha-glucuronidase (TM0752) in complex with NADH and D-glucuronic acid

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

Alpha-glucosidase, putative

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

7ctm__assembly_1__model_1

7ctm__assembly_1__model_1 | I(q)

7ctm__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 (5)

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 water

7. Citations (1)

Crystal structure of Thermotoga maritima alpha-glucuronidase (TM0752) in complex with NADH and D-glucuronic acid

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

Alpha-glucosidase, putative

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

7ctm__assembly_1__model_1

7ctm__assembly_1__model_1 | I(q)

7ctm__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 (5)

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 water

7. Citations (1)