SAXSdb — 2cnm

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

MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18

SALMONELLA TYPHIMURIUM LT2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	30S RIBOSOMAL PROTEIN S18 × 1 （V2H9S5） COENZYME A × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	30S RIBOSOMAL PROTEIN S18 × 1 （V2H9S5） COENZYME A × 1 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	30S RIBOSOMAL PROTEIN S18 × 1 （V2H9S5） COENZYME A × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8ZJW4_SALTY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–148； UniProt 1–148 Author chain B； PDBConstruct 1–148； UniProt 1–148 Author chain C； PDBConstruct 1–148； UniProt 1–148

30S RIBOSOMAL PROTEIN S18

OrganismNot specified

UniProt V2H9S5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18 × 1 （Q8ZJW4） COENZYME A × 1 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18 × 1 （Q8ZJW4） COENZYME A × 1 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18 × 1 （Q8ZJW4） COENZYME A × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	V2H9S5_SALET
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 2–7； UniProt 2–7 Author chain E； PDBConstruct 2–7； UniProt 2–7 Author chain F； PDBConstruct 2–7； UniProt 2–7

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	2cnm
Deposition date deposition_date	2006-05-22
Structure title title	RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).
Keywords keywords	N-ALPHA ACETYLATION, GCN5-N-ACETYLTRANSFERASE, RIBOSOMAL PROTEIN, ACETYLTRANSFERASE, GNAT, TRANSFERASE, ACYLTRANSFERASE; 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.

2cnm__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2cnm__assembly_3__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2cnm__assembly_3__model_1 | P(r) · Pending

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

Rg（Guinier）	16.66 Å
Rg (electron density)	15.22 Å
Total Rg	16.45 Å
Atom count	1315
Residues	157
Excluded volume	23275 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2cnm__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2cnm__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2cnm__assembly_3__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 (4)

Entity 1 Entity 1 polymer

Description description	MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18
Molecular weight formula_weight	18325.8 kDa
EC 编号 ec_number	2.3.1.128
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	4005

MNTISILSTTDLPAAWQIEQRAHAFPWSEKTFFGNQGERYLNLKLTADDRMAAFAITQVVLDEATLFNIAVDPDFQRRGLGRMLLEHLIDELETRGVVTLWLEVRASNAAAIALYESLGFNEATIRRNYYPTAQGHEDAIIMALPISMKLHHHHHHHHHH

Source Source

Source organism organism	SALMONELLA TYPHIMURIUM LT2
NCBI taxonomy ID ncbi_taxonomy_id	99287
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	30S RIBOSOMAL PROTEIN S18
Molecular weight formula_weight	897.1 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

XARYFRR

Entity 3 Entity 3 non-polymer

Description description	COENZYME A
Molecular weight formula_weight	767.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	60

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6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	2cnmA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

Domain ID domain_id	2cnmB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

Domain ID domain_id	2cnmC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

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Unit-cell length a length_a	133.127 Å
Unit-cell length b length_b	133.127 Å
Unit-cell length c length_c	190.986 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	54

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	98.530 Å
R factor r_factor	0.1960
R_work r_work	0.1930
R_free r_free	0.2570

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).

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

MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18

State in the Current Structure

Other States of the Same Protein in the Database

30S RIBOSOMAL PROTEIN S18

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

2cnm__assembly_3__model_1

2cnm__assembly_3__model_1 | I(q)

2cnm__assembly_3__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).

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

MODIFICATION OF 30S RIBOSOMAL SUBUNIT PROTEIN S18

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

30S RIBOSOMAL PROTEIN S18

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

2cnm__assembly_3__model_1

2cnm__assembly_3__model_1 | I(q)

2cnm__assembly_3__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)