SAXSdb — 3bss

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

Acetyltransferase

Campylobacter jejuni

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q0P9D1_CAMJE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–198； UniProt 1–195

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	3bss
Deposition date deposition_date	2007-12-26
Structure title title	PglD from Campylobacter jejuni, NCTC 11168, with native substrate
Keywords keywords	;left-hand beta helix, hexapeptide repeat, UDP, acetyl coenzyme Z, Rossmann fold, bacillosamine, campylobacter, pgl, N-linked glycosylation, 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.

3bss__assembly_1__model_1

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

Download this curve (.dat)

3bss__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3bss__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.19 Å
Rg (electron density)	24.46 Å
Total Rg	25.16 Å
Atom count	4449
Residues	582
Excluded volume	79870 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3bss__assembly_1__model_1`	trimeric （3）	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	Acetyltransferase
Molecular weight formula_weight	21390.0 kDa
EC 编号 ec_number	2.7.7.23
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	1685

GSAMARTEKIYIYGASGHGLVCEDVAKNMGYKECIFLDDFKGMKFESTLPKYDFFIAIGNNEIRKKIYQKISENGFKIVNLIHKSALISPSAIVEENAGILIMPYVVINAKAKIEKGVILNTSSVIEHECVIGEFSHVSVGAKCAGNVKIGKNCFLGINSCVLPNLSLADDSILGGGATLVKNQDEKGVFVGVPAKRM

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	UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose
Molecular weight formula_weight	590.4 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	202

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3bssa_
Class class	b — All beta proteins
Fold Fold fold	b.81 — Single-stranded left-handed beta-helix
Superfamily Superfamily superfamily	b.81.1 — Trimeric LpxA-like enzymes
Family Family family	b.81.1.8 — PglD-like

CATH v4.4 (2 domains)

Domain ID domain_id	3bssA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	3bssA02
Class class	2 — Mainly Beta
Architecture architecture	160 — 3 Solenoid
Topology topology	10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily	10 — Hexapeptide repeat proteins

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Unit-cell length a length_a	162.338 Å
Unit-cell length b length_b	162.338 Å
Unit-cell length c length_c	162.338 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	24

Space group space_group	P 43 3 2
Space-group number int_tables_number	212
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	29.640 Å
R factor r_factor	0.1780
R_work r_work	0.1780
R_free r_free	0.1910

PglD from Campylobacter jejuni, NCTC 11168, with native substrate

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

Acetyltransferase

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

3bss__assembly_1__model_1

3bss__assembly_1__model_1 | I(q)

3bss__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) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)

PglD from Campylobacter jejuni, NCTC 11168, with native substrate

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

Acetyltransferase

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

3bss__assembly_1__model_1

3bss__assembly_1__model_1 | I(q)

3bss__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) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)