SAXSdb — 11tv

▼

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

alpha/beta-hydrolase macrolide esterase EstX

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	;(3~{R},4~{S},5~{S},6~{R},8~{R},10~{E},12~{E},14~{R},15~{R})-14-[[(2~{R},3~{R},4~{R},5~{R},6~{R})-3,4-dimethoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[(2~{R},3~{R},4~{R},5~{S},6~{R})-4-(dimethylamino)-5-[(2~{S},4~{R},5~{S},6~{S})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-3-oxidanyl-oxan-2-yl]oxy-4,8,12-trimethyl-3,15-bis(oxidanyl)-9-oxidanylidene-6-(2-oxidanylideneethyl)heptadeca-10,12-dienoic acid ; × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	;(3~{R},4~{S},5~{S},6~{R},8~{R},10~{E},12~{E},14~{R},15~{R})-14-[[(2~{R},3~{R},4~{R},5~{R},6~{R})-3,4-dimethoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[(2~{R},3~{R},4~{R},5~{S},6~{R})-4-(dimethylamino)-5-[(2~{S},4~{R},5~{S},6~{S})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-3-oxidanyl-oxan-2-yl]oxy-4,8,12-trimethyl-3,15-bis(oxidanyl)-9-oxidanylidene-6-(2-oxidanylideneethyl)heptadeca-10,12-dienoic acid ; × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q75WM3_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–280； UniProt 1–280 Author chain D； PDBConstruct 1–280； UniProt 1–280

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	11tv
Deposition date deposition_date	2026-03-12
Last revision last_revision	2026-04-08
Structure title title	Crystal structure of alpha/beta-hydrolase macrolide esterase EstX from Escherichia coli (S102A mutant) in complex with linearized tylosin
Keywords keywords	alpha/beta-hydrolase, esterase, macrolide resistance, 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.

11tv__assembly_1__model_1

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

Download this curve (.dat)

11tv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

11tv__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	18.64 Å
Rg (electron density)	17.34 Å
Total Rg	18.37 Å
Atom count	2312
Residues	280
Excluded volume	39278 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`11tv__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`11tv__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	alpha/beta-hydrolase macrolide esterase EstX
Molecular weight formula_weight	31058.2 kDa
Mutation mutation	S102A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,A
Atom count atom_count	4933

MKEKVVVDKAISLYTESFGDPAHEPIILIMGAMSSAVWWPDEFCSQLAKMGRYVIRYDHRDTGKSTSYEPGQAPYSVEELADDVVRVIDGYGLEAAHLVGMALGGFLSQLVALKYPKRVKSLTLIASERLADADPDMPAFDPAIIEYHQRAESLDWSDRDAVVAYQVGAWRINSGTAHAFDAEKIQNIAELNFDRTPNILTTFNHTTLGGGERWLGRLNEIAVPTLIIHGTEDPVLPYVHGLALKDAIRGSKMLTLEGTGHELHHEDWPRIIQAIKGQTS

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli BL21

Entity 2 Entity 2 non-polymer

Description description	;(3~{R},4~{S},5~{S},6~{R},8~{R},10~{E},12~{E},14~{R},15~{R})-14-[[(2~{R},3~{R},4~{R},5~{R},6~{R})-3,4-dimethoxy-6-methyl-5-oxidanyl-oxan-2-yl]oxymethyl]-5-[(2~{R},3~{R},4~{R},5~{S},6~{R})-4-(dimethylamino)-5-[(2~{S},4~{R},5~{S},6~{S})-4,6-dimethyl-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-3-oxidanyl-oxan-2-yl]oxy-4,8,12-trimethyl-3,15-bis(oxidanyl)-9-oxidanylidene-6-(2-oxidanylideneethyl)heptadeca-10,12-dienoic acid ;
Molecular weight formula_weight	934.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	324

▶

Unit-cell length a length_a	44.594 Å
Unit-cell length b length_b	72.691 Å
Unit-cell length c length_c	82.051 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	95.73 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	29.020 Å
R factor r_factor	0.1654
R_work r_work	0.1642
R_free r_free	0.1988

Crystal structure of alpha/beta-hydrolase macrolide esterase EstX from Escherichia coli (S102A mutant) in complex with linearized tylosin

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

alpha/beta-hydrolase macrolide esterase EstX

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

11tv__assembly_1__model_1

11tv__assembly_1__model_1 | I(q)

11tv__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)

Crystal structure of alpha/beta-hydrolase macrolide esterase EstX from Escherichia coli (S102A mutant) in complex with linearized tylosin

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

alpha/beta-hydrolase macrolide esterase EstX

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

11tv__assembly_1__model_1

11tv__assembly_1__model_1 | I(q)

11tv__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)