SAXSdb — 9jc2

▼

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

ATP synthase gamma chain

Bacillus sp. PS3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	ATP synthase subunit a × 3 ATP synthase epsilon chain × 1 （A0A0M5MQR7） ATP synthase subunit b × 6 ATP synthase subunit c × 10 （P00845）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0M4TPJ7_BACP3
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–285； UniProt 1–285

ATP synthase epsilon chain

Bacillus sp. PS3

UniProt A0A0M5MQR7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	ATP synthase subunit a × 3 ATP synthase gamma chain × 1 （A0A0M4TPJ7） ATP synthase subunit b × 6 ATP synthase subunit c × 10 （P00845）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0M5MQR7_BACP3
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain E； PDBConstruct 1–87； UniProt 1–87

ATP synthase subunit c

Bacillus sp. PS3

UniProt P00845

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 21	ATP synthase subunit a × 3 ATP synthase gamma chain × 1 （A0A0M4TPJ7） ATP synthase epsilon chain × 1 （A0A0M5MQR7） ATP synthase subunit b × 6	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPL_BACP3
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain L； PDBConstruct 1–72； UniProt 1–72 Author chain M； PDBConstruct 1–72； UniProt 1–72 Author chain N； PDBConstruct 1–72； UniProt 1–72 Author chain O； PDBConstruct 1–72； UniProt 1–72 Author chain P； PDBConstruct 1–72； UniProt 1–72 Author chain Q； PDBConstruct 1–72； UniProt 1–72 Author chain R； PDBConstruct 1–72； UniProt 1–72 Author chain S； PDBConstruct 1–72； UniProt 1–72 Author chain T； PDBConstruct 1–72； UniProt 1–72 Author chain U； PDBConstruct 1–72； UniProt 1–72

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9jc2
Deposition date deposition_date	2024-08-28
Structure title title	Engineering of ATP synthase Fo
Keywords keywords	Molecular Motor, ATP synthase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9jc2__assembly_1__model_1

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

Download this curve (.dat)

9jc2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9jc2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	42.08 Å
Rg (electron density)	40.89 Å
Total Rg	40.98 Å
Atom count	10815
Residues	1875
Excluded volume	185700 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9jc2__assembly_1__model_1`	21-meric （21）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	ATP synthase subunit a
Molecular weight formula_weight	26449.3 kDa
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	10815

MEHKAPLVEFLGLTFNLSDMLMITITCLIVFIIAVAATRSLQLRPTGMQNFMEWVFDFVRGIINSTMDWQTGGRFLTLGVTLIMYVFVANMLGLPFSVHVNGELWWKSPTADATVTLTLAVMVVALTHYYGVKMKGASDYLRDYTRPVAWLFPLKIIEEFANTLTLGLRLFGNIYAGEILLGLLASLGTHYGVLGAVGAAIPMMVWQAFSIFVGTIQAFIFTMLTMVYMAHKVSHDH

Source Source

Source organism organism	Bacillus sp. PS3
NCBI taxonomy ID ncbi_taxonomy_id	2334
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	ATP synthase gamma chain
Molecular weight formula_weight	31859.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MASLRDIKTRINATKKTSQITKAMEMVSTSKLNRAEQNAKSFVPYMEKIQEVVANVALGAGGASHPMLVSRPVKKTGYLVITSDRGLAGAYNSNVLRLVYQTIQKRHASPDEYAIIVIGRVGLSFFRKRNMPVILDITRLPDQPSFADIKEIARKTVGLFADGTFDELYMYYNHYVSAIQQEVTERKLLPLTDLAENKQRTVYEFEPSQEEILDVLLPQYAESLIYGALLDAKASEHAARMTAMKNATDNANELIRTLTLSYNRARQAAITQEITEIVAGANALQ

Source Source

Source organism organism	Bacillus sp. PS3
NCBI taxonomy ID ncbi_taxonomy_id	2334
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	ATP synthase epsilon chain
Molecular weight formula_weight	9221.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

MKTIHVSVVTPDGPVYEDDVEMVSVKAKSGELGILPGHIPLVAPLEISAARLKKGGKTQYIAVSGGFLEVRPDKVTILAQAAERAED

Source Source

Source organism organism	Bacillus sp. PS3
NCBI taxonomy ID ncbi_taxonomy_id	2334
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	ATP synthase subunit b
Molecular weight formula_weight	19437.4 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,G,H,I,J,K

MGEAAHGISGGTIIYQLLMFIILLALLRKFAWQPLMNIMKQREEHIANEIDQAEKRRQEAEKLLEEQRELMKQSRQEAQALIENARKLAEEQKEQIVASARAEAERVKETAKKEIEREKEQAMAALREQVASLSVLIASKVIEKELTEQDQRKLIEAYIKDVQEVGGAR

Source Source

Source organism organism	Bacillus sp. PS3
NCBI taxonomy ID ncbi_taxonomy_id	2334
Host organism host_organism	Escherichia coli

Entity 5 Entity 5 polymer

Description description	ATP synthase subunit c
Molecular weight formula_weight	7337.8 kDa
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,M,N,O,P,Q,R,S,T,U

MSLGVLAAAIAVGLGALGAGIGNGLIVSRTIEGIARQPELRPVLQTTMFIGVALVEALPIIGVVFSFIYLGR

Source Source

Source organism organism	Bacillus sp. PS3
NCBI taxonomy ID ncbi_taxonomy_id	2334
Host organism host_organism	Escherichia coli

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	3.96 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	32633

Engineering of ATP synthase Fo

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

ATP synthase gamma chain

State in the Current Structure

Other States of the Same Protein in the Database

ATP synthase epsilon chain

State in the Current Structure

Other States of the Same Protein in the Database

ATP synthase subunit c

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

9jc2__assembly_1__model_1

9jc2__assembly_1__model_1 | I(q)

9jc2__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

7. Citations (1)

Engineering of ATP synthase Fo

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

ATP synthase gamma chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ATP synthase epsilon chain

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

ATP synthase subunit c

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

9jc2__assembly_1__model_1

9jc2__assembly_1__model_1 | I(q)

9jc2__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 polymer

Polymer Polymer

Source Source

7. Citations (1)