SAXSdb — 1mo2

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

Erythronolide synthase, modules 5 and 6

Saccharopolyspora erythraea

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ERYA3_SACER
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–283； UniProt 2893–3172 Author chain B； PDBConstruct 4–283； UniProt 2893–3172

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	1mo2
Deposition date deposition_date	2002-09-05
Structure title title	Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5
Keywords keywords	;Thioesterase, Polyketide Synthase, open substrate channel, TE, PKS, alpha beta hydrolase, 6-deoxyerythronolide, picromycin, pikromycin, erythromycin, TRANSFERASE ;; TRANSFERASE
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.

1mo2__assembly_1__model_1

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

Download this curve (.dat)

1mo2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1mo2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	30.48 Å
Rg (electron density)	30.20 Å
Total Rg	30.63 Å
Atom count	3774
Residues	502
Excluded volume	66453 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1mo2__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 (2)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1mo2a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.22 — Thioesterase domain of polypeptide, polyketide and fatty acid synthases

Domain ID domain_id	d1mo2b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.22 — Thioesterase domain of polypeptide, polyketide and fatty acid synthases

CATH v4.4 (2 domains)

Domain ID domain_id	1mo2A00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

Domain ID domain_id	1mo2B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

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Unit-cell length a length_a	80.500 Å
Unit-cell length b length_b	102.500 Å
Unit-cell length c length_c	156.500 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 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2445
R_work r_work	0.2422
R_free r_free	0.2866

Description description	Erythronolide synthase, modules 5 and 6
Molecular weight formula_weight	31283.9 kDa
EC 编号 ec_number	2.3.1.94
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	3830

Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5

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

Erythronolide synthase, modules 5 and 6

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

1mo2__assembly_1__model_1

1mo2__assembly_1__model_1 | I(q)

1mo2__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Source organism organism	Saccharopolyspora erythraea
NCBI taxonomy ID ncbi_taxonomy_id	1836
Host organism host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	56

Thioesterase Domain from 6-Deoxyerythronolide Synthase (DEBS TE), pH 8.5

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

Erythronolide synthase, modules 5 and 6

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

1mo2__assembly_1__model_1

1mo2__assembly_1__model_1 | I(q)

1mo2__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)