SAXSdb — 3h7q

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

Holo-[acyl-carrier-protein] synthase

Mycobacterium tuberculosis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	BICINE × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACPS_MYCTU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–132； UniProt 1–130

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	3h7q
Deposition date deposition_date	2009-04-28
Structure title title	Crystal structure of the holo-[Acyl-Carrier-Protein] Synthase (ACPS) from Mycobacterium tuberculosis
Keywords keywords	;Homo-trimer, 9-stand pseudo beta barrel protein, Cytoplasm, Fatty acid biosynthesis, Lipid synthesis, Magnesium, Metal-binding, 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.

3h7q__assembly_1__model_1

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

Download this curve (.dat)

3h7q__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3h7q__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	21.86 Å
Rg (electron density)	20.42 Å
Total Rg	21.25 Å
Atom count	2664
Residues	360
Excluded volume	47048 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3h7q__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	Holo-[acyl-carrier-protein] synthase
Molecular weight formula_weight	14147.9 kDa
EC 编号 ec_number	2.7.8.7
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	935

GAMGIVGVGIDLVSIPDFAEQVDQPGTVFAETFTPGERRDASDKSSSAARHLAARWAAKEAVIKAWSGSRFAQRPVLPEDIHRDIEVVTDMWGRPRVRLTGAIAEYLADVTIHVSLTHEGDTAAAVAILEAP

Source Source

Source organism organism	Mycobacterium tuberculosis
NCBI taxonomy ID ncbi_taxonomy_id	1773
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	BICINE
Molecular weight formula_weight	163.2 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	47

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d3h7qa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.150 — 4'-phosphopantetheinyl transferase
Superfamily Superfamily superfamily	d.150.1 — 4'-phosphopantetheinyl transferase
Family Family family	d.150.1.0 — automated matches

Domain ID domain_id	d3h7qa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	3h7qA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	470 — Ribosomal Protein L22; Chain A
Homologous superfamily homologous superfamily	20 — 4'-phosphopantetheinyl transferase domain

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Unit-cell length a length_a	68.810 Å
Unit-cell length b length_b	68.810 Å
Unit-cell length c length_c	86.840 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	9

Space group space_group	H 3
Space-group number int_tables_number	146
Crystal system crystal_system	—

Resolution resolution	2.250 Å
Low-resolution limit resolution_low	24.568 Å
R factor r_factor	0.2070
R_work r_work	0.2040
R_free r_free	0.2490

Crystal structure of the holo-[Acyl-Carrier-Protein] Synthase (ACPS) from Mycobacterium tuberculosis

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

Holo-[acyl-carrier-protein] synthase

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

3h7q__assembly_1__model_1

3h7q__assembly_1__model_1 | I(q)

3h7q__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 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Crystal structure of the holo-[Acyl-Carrier-Protein] Synthase (ACPS) from Mycobacterium tuberculosis

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

Holo-[acyl-carrier-protein] synthase

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

3h7q__assembly_1__model_1

3h7q__assembly_1__model_1 | I(q)

3h7q__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 (2 domains)

CATH v4.4 (1 domains)

7. Citations (1)