1f7t

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A

Method: X-RAY DIFFRACTION

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

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE

Bacillus subtilis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	SODIUM ION × 5 CHLORIDE ION × 11 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 2 GLYCEROL × 1 water × 3	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 3	SODIUM ION × 3 CHLORIDE ION × 8 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 3 GLYCEROL × 1 water × 3	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 6	SODIUM ION × 8 CHLORIDE ION × 19 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 5 GLYCEROL × 2 water × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACPS_BACSU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–122； UniProt 2–121 Author chain B； PDBConstruct 3–122； UniProt 2–121 Author chain C； PDBConstruct 3–122； UniProt 2–121 Author chain D； PDBConstruct 3–122； UniProt 2–121 Author chain E； PDBConstruct 3–122； UniProt 2–121 Author chain F； PDBConstruct 3–122； UniProt 2–121

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	1f7t
Deposition date deposition_date	2000-06-27
Structure title title	HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A
Keywords keywords	9-strand pseudo beta barrel, LIPID SYNTHESIS, 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.

1f7t__assembly_1__model_1

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

Download this curve (.dat)

1f7t__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1f7t__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	21.64 Å
Rg (electron density)	20.31 Å
Total Rg	21.20 Å
Atom count	2828
Residues	357
Excluded volume	50720 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1f7t__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1f7t__assembly_2__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1f7t__assembly_3__model_1`	hexameric （6）	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 (6)

Entity 1 Entity 1 polymer

Description description	HOLO-(ACYL CARRIER PROTEIN) SYNTHASE
Molecular weight formula_weight	13691.7 kDa
EC 编号 ec_number	2.7.8.7
Mutation mutation	Q96P
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	6141

GGIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKDQNGKPYIICTKLSPAAVHVSITHTKEYAAAQVVIERLSS

Source Source

Source organism organism	Bacillus subtilis
NCBI taxonomy ID ncbi_taxonomy_id	1423
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	19

Entity 4 Entity 4 non-polymer

Description description	2,3-DIHYDROXY-1,4-DITHIOBUTANE
Molecular weight formula_weight	154.3 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	469

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6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (12 domains)

Domain ID domain_id	d1f7ta1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7ta2
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

Domain ID domain_id	d1f7tb1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7tb2
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

Domain ID domain_id	d1f7tc1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7tc2
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

Domain ID domain_id	d1f7td1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7td2
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

Domain ID domain_id	d1f7te1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7te2
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

Domain ID domain_id	d1f7tf1
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.150.1.2 — Holo-(acyl carrier protein) synthase ACPS

Domain ID domain_id	d1f7tf2
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 (6 domains)

Domain ID domain_id	1f7tA00
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

Domain ID domain_id	1f7tB00
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

Domain ID domain_id	1f7tC00
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

Domain ID domain_id	1f7tD00
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

Domain ID domain_id	1f7tE00
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

Domain ID domain_id	1f7tF00
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	76.262 Å
Unit-cell length b length_b	76.160 Å
Unit-cell length c length_c	85.693 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.32 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1970
R_work r_work	0.1960
R_free r_free	0.2190

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A

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

1f7t__assembly_1__model_1

1f7t__assembly_1__model_1 | I(q)

1f7t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (12 domains)

CATH v4.4 (6 domains)

7. Citations (1)

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE AT 1.8A

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

1f7t__assembly_1__model_1

1f7t__assembly_1__model_1 | I(q)

1f7t__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (12 domains)

CATH v4.4 (6 domains)

7. Citations (1)