7xrm

Ethanolamine ammonia-lyase complexed with AdoMeCbl

Method: X-RAY DIFFRACTION

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

Ethanolamine ammonia-lyase large subunit

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	Ethanolamine ammonia-lyase small subunit × 6 （P19636） GLYCEROL × 33 AMMONIUM ION × 6 (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol × 6 COBALAMIN × 6 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EUTB_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–453； UniProt 1–453 Author chain C； PDBConstruct 1–453； UniProt 1–453

Ethanolamine ammonia-lyase small subunit

Escherichia coli

UniProt P19636

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	Ethanolamine ammonia-lyase large subunit × 6 （P0AEJ6） GLYCEROL × 33 AMMONIUM ION × 6 (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol × 6 COBALAMIN × 6 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	EUTC_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 12–263； UniProt 44–295 Author chain D； PDBConstruct 12–263； UniProt 44–295

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	7xrm
Deposition date deposition_date	2022-05-10
Structure title title	Ethanolamine ammonia-lyase complexed with AdoMeCbl
Keywords keywords	Adenosylcobalamin, Radical enzyme, LYASE; LYASE
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.

7xrm__assembly_1__model_1

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

Download this curve (.dat)

7xrm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7xrm__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	51.66 Å
Rg (electron density)	51.53 Å
Total Rg	51.81 Å
Atom count	33174
Residues	4233
Excluded volume	590470 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7xrm__assembly_1__model_1`	dodecameric （12）	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 (7)

Entity 1 Entity 1 polymer

Description description	Ethanolamine ammonia-lyase large subunit
Molecular weight formula_weight	49447.8 kDa
EC 编号 ec_number	4.3.1.7
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	11814

MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEDDCVTRLIQDDVNETAYNQIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGAKKMPVIKKANTTIGIPGTFSARLQPNDTRDDVQSIAAQIYEGLSFGVGDAVIGVNPVTDDVENLSRVLDTIYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDPFIVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLESMGIMANGRLTKRAGDPSLFF

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 polymer

Description description	Ethanolamine ammonia-lyase small subunit
Molecular weight formula_weight	28769.0 kDa
EC 编号 ec_number	4.3.1.7
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

MDQSSHHHHHHALDLGSAEAKAWIGVENPHRADVLTELRRSTVARVCTGRAGPRPRTQALLRFLADHSRSKDTVLKEVPEEWVKAQGLLEVRSEISDKNLYLTRPDMGRRLCAEAVEALKAQCVANPDVQVVISDGLSTDAITVNYEEILPPLMAGLKQAGLKVGTPFFVRYGRVKIEDQIGEILGAKVVILLVGERPGLGQSESLSCYAVYSPRMATTVEADRTCISNIHQGGTPPVEAAAVIVDLAKRMLEQKASGINMTR

Source Source

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

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 4 Entity 4 non-polymer

Description description	AMMONIUM ION
Molecular weight formula_weight	18.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-ethyl-oxolane-3,4-diol
Molecular weight formula_weight	265.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 non-polymer

Description description	COBALAMIN
Molecular weight formula_weight	1330.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	651

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Unit-cell length a length_a	242.885 Å
Unit-cell length b length_b	242.885 Å
Unit-cell length c length_c	76.638 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 63
Space-group number int_tables_number	173
Crystal system crystal_system	hexagonal

Resolution resolution	2.130 Å
Low-resolution limit resolution_low	46.420 Å
R factor r_factor	0.1962
R_work r_work	0.1942
R_free r_free	0.2198

Ethanolamine ammonia-lyase complexed with AdoMeCbl

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

Ethanolamine ammonia-lyase large subunit

State in the Current Structure

Other States of the Same Protein in the Database

Ethanolamine ammonia-lyase small subunit

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

7xrm__assembly_1__model_1

7xrm__assembly_1__model_1 | I(q)

7xrm__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)

Ethanolamine ammonia-lyase complexed with AdoMeCbl

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

Ethanolamine ammonia-lyase large subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Ethanolamine ammonia-lyase small subunit

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

7xrm__assembly_1__model_1

7xrm__assembly_1__model_1 | I(q)

7xrm__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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Citations (1)