SAXSdb — 2ref

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

CurA

Lyngbya majuscula

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ACETYL COENZYME *A × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	ACETYL 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	Q6DNF2_9CYAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–224； UniProt 219–439 Author chain B； PDBConstruct 4–224； UniProt 219–439

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	2ref
Deposition date deposition_date	2007-09-26
Structure title title	Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula soaked with malonyl-CoA
Keywords keywords	GNAT, CURACIN, S-ACETYLTRANSFERASE, DECARBOXYLASE, POLYKETIDE SYNTHASE, LOADING, Phosphopantetheine, TRANSFERASE, LYASE; TRANSFERASE, 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.

2ref__assembly_1__model_1

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

Download this curve (.dat)

2ref__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ref__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	17.99 Å
Rg (electron density)	16.76 Å
Total Rg	17.74 Å
Atom count	1706
Residues	203
Excluded volume	30361 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ref__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2ref__assembly_2__model_1`	monomeric （1）	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	CurA
Molecular weight formula_weight	25913.6 kDa
EC 编号 ec_number	2.3.1.38, 4.1.1.9
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	3510

SNASLNCFENNYYNLRHPKIEDLRDLIALETLCWSENLQVDNEEIYRRIFKIPQGQFILELEDKIVGAIYSQRIDNPQLLDNKTCTQVPLLHTESGVVVQLLAVNILPELQNQGLGDRLLEFMLQYCAQISGVEKVVAVTLCRNYPDYSPMPMAEYIHQKNESGLLVDPLLRFHQIHGAKIEKLLPGYRPKDWENQTCGVLVSYDIQHRQRFDGATVEKNRQTK

Source Source

Source organism organism	Lyngbya majuscula
NCBI taxonomy ID ncbi_taxonomy_id	276768
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	ACETYL COENZYME *A
Molecular weight formula_weight	809.6 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	4

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6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	2refA01
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	2refB01
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	91.886 Å
Unit-cell length b length_b	91.886 Å
Unit-cell length c length_c	139.486 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 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.750 Å
Low-resolution limit resolution_low	46.500 Å
R factor r_factor	0.2100
R_work r_work	0.2070
R_free r_free	0.2510

Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula soaked with malonyl-CoA

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

CurA

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

2ref__assembly_1__model_1

2ref__assembly_1__model_1 | I(q)

2ref__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) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula soaked with malonyl-CoA

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

CurA

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

2ref__assembly_1__model_1

2ref__assembly_1__model_1 | I(q)

2ref__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) 2 domains

CATH v4.4 (2 domains)

7. Citations (1)