SAXSdb — 4ztc

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

Aminotransferase homolog

Campylobacter jejuni

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	;[(2R,3R,4R,5S,6R)-3-acetamido-6-methyl-5-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-4-oxidanyl-oxan-2-yl] [[(2R,3S,4R,5R)-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] hydrogen phosphate ; × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9S5Y7_CAMJU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–386； UniProt 1–386

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	4ztc
Deposition date deposition_date	2015-05-14
Structure title title	PglE Aminotransferase in complex with External Aldimine, Mutant K184A
Keywords keywords	;aminotransferase, N-N'-diacetylbacillosamine, N-glycosylation pyridoxyl 5'-phosphate, 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.

4ztc__assembly_1__model_1

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

Download this curve (.dat)

4ztc__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4ztc__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.01 Å
Rg (electron density)	27.41 Å
Total Rg	28.21 Å
Atom count	6256
Residues	770
Excluded volume	112160 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4ztc__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 (3)

Entity 1 Entity 1 polymer

Description description	Aminotransferase homolog
Molecular weight formula_weight	43799.2 kDa
Mutation mutation	K184A
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	3416

MRFFLSPPHMGGNELKYIEEVFKSNYIAPLGEFVNRFEQSVKDYSKSENALALNSATAALHLALRVAGVKQDDIVLASSFTFIASVAPICYLKAKPVFIDCDETYNIDVDLLKLAIKECEKKPKALILTHLYGNAAKMDEIVEICKENDIVLIEDAAEALGSFYKNKALGTFGEFGVYSYNGNAIITTSGGGMLIGKNKEKIEKARFYSTQARENCLHYEHLDYGYNYRLSNVLGAIGVAQMEVLEQRVLKKREIYEWYKEFLGEYFSFLDELENSRSNRWLSTALINFDKNELNSCQKDINISQKNITLHPKISKLIEDLKNKQIETRPLWKTMHAQEVFKGAKAYLNGNSELFFQKGICLPSGTAMSKDDVYEISKLILKSIKA

Source Source

Source organism organism	Campylobacter jejuni
NCBI taxonomy ID ncbi_taxonomy_id	197
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;[(2R,3R,4R,5S,6R)-3-acetamido-6-methyl-5-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-4-oxidanyl-oxan-2-yl] [[(2R,3S,4R,5R)-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] hydrogen phosphate ;
Molecular weight formula_weight	819.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	275

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6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d4ztca_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.4 — GABA-aminotransferase-like

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Unit-cell length a length_a	66.161 Å
Unit-cell length b length_b	66.161 Å
Unit-cell length c length_c	169.013 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 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	29.610 Å
R factor r_factor	0.1918
R_work r_work	0.1883
R_free r_free	0.2545

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

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

Aminotransferase homolog

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

4ztc__assembly_1__model_1

4ztc__assembly_1__model_1 | I(q)

4ztc__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

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

7. Citations (1)

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

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

Aminotransferase homolog

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

4ztc__assembly_1__model_1

4ztc__assembly_1__model_1 | I(q)

4ztc__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

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

7. Citations (1)