9jc1

Engineering of ATP synthase

Method: ELECTRON MICROSCOPY

▼

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

ATP synthase subunit beta

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 14	ATP synthase gamma chain × 1 （A0A0M4TPJ7） ATP synthase epsilon chain × 1 （A0A0M5MQR7） ATP synthase delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha × 3 （A0A0M3VGF9） ATP synthase subunit b × 3 ATP synthase subunit b × 3 ADENOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0M4U1P9_BACP3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain D； PDBConstruct 12–484； UniProt 1–473 Author chain E； PDBConstruct 12–484； UniProt 1–473 Author chain F； PDBConstruct 12–484； UniProt 1–473

ATP synthase gamma chain

Bacillus sp. PS3

UniProt A0A0M4TPJ7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 14	ATP synthase subunit beta × 3 （A0A0M4U1P9） ATP synthase epsilon chain × 1 （A0A0M5MQR7） ATP synthase delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha × 3 （A0A0M3VGF9） ATP synthase subunit b × 3 ATP synthase subunit b × 3 ADENOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 4	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 G； 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 14	ATP synthase subunit beta × 3 （A0A0M4U1P9） ATP synthase gamma chain × 1 （A0A0M4TPJ7） ATP synthase delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha × 3 （A0A0M3VGF9） ATP synthase subunit b × 3 ATP synthase subunit b × 3 ADENOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 4	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 H； PDBConstruct 1–87； UniProt 1–87

ATP synthase delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha

Bacillus sp. PS3

UniProt A0A0M3VGF9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 14	ATP synthase subunit beta × 3 （A0A0M4U1P9） ATP synthase gamma chain × 1 （A0A0M4TPJ7） ATP synthase epsilon chain × 1 （A0A0M5MQR7） ATP synthase subunit b × 3 ATP synthase subunit b × 3 ADENOSINE-5'-DIPHOSPHATE × 1 MAGNESIUM ION × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A0M3VGF9_BACP3
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain I； PDBConstruct 80–580； UniProt 2–502 Author chain J； PDBConstruct 80–580； UniProt 2–502 Author chain K； PDBConstruct 80–580； UniProt 2–502

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	9jc1
Deposition date deposition_date	2024-08-28
Structure title title	Engineering of ATP synthase
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.

9jc1__assembly_1__model_1

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

Download this curve (.dat)

9jc1__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9jc1__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	50.17 Å
Rg (electron density)	49.26 Å
Total Rg	49.25 Å
Atom count	28159
Residues	3905
Excluded volume	498770 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9jc1__assembly_1__model_1`	tetradecameric （14）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	ATP synthase subunit beta
Molecular weight formula_weight	53424.6 kDa
EC 编号 ec_number	7.1.2.2
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F
Atom count atom_count	28164

MHHHHHHHHHHMTRGRVIQVMGPVVDVKFENGHLPAIYNALKIQHKARNENEVDIDLTLEVALHLGDDTVRTIAMASTDGLIRGMEVIDTGAPISVPVGEVTLGRVFNVLGEPIDLEGDIPADARRDPIHRPAPKFEELATEVEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYHEMKDSGVISKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTAKGSITSIQAIYVPADDYTDPAPATTFSHLDATTNLERKLAEMGIYPAVDPLASTSRALAPEIVGEEHYQVARKVQQTLQRYKELQDIIAILGMDELSDEDKLVVHRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVRGFKEILEGKYDHLPEDAFRLVGRIEEVVEKAKAMGVEV

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	G

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	H

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 delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha
Molecular weight formula_weight	63248.1 kDa
EC 编号 ec_number	7.1.2.2
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

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

MGIAKAVAYSARPLTDEELRALSDVFAQKVGKQTLEIENIIDPELIGGVRLRIGNRIYDGSVSGQLERIRRQLIGGSGGSIRAEEISALIKQQIENYESQIQVSDVGTVIQVGDGIARAHGLDNVMSGELVEFANGVMGMALNLEENNVGIVILGPYTGIKEGDEVRRTGRIMEVPVGEALIGRVVNPLGQPVDGLGPVETTETRPIESPAPGVMDRRSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTSVAIDTIINQKDQNMISIYVAIGQKESTVRTVVETLRKHGALDYTIVVTASASQPAPLLFLAPYAGVAMGEYFMYKGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINAGLSVSRVGGAAQIKAMKKVAGTLRLDLAAYRELEAFAQFGSDLDKATQAKLARGARTVEVLKQDLHQPIPVEKQVLIIYALTRGFLDDIPVEDVRRFEKEFYLFLDQNGQHLLEHIRTTKDLPNEDDLNKAIEAFKKTFVVSQ

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 b
Molecular weight formula_weight	18601.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,M

MGEAAHGISGGTIIYQLLMFIILLALLRKFAWQPLMNIMKQREEHIANEIDQAEKRRQEAEKLLEEQRELMKQSRQEAQALIENARKLAEEQKEQIVASARAEAERVKETAKKEIEREKEQAMAALREQVASLSVLIASKVIXXXXXXXXXXXXXXXXXXXXXXXXXXX

Source Source

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

Entity 6 Entity 6 polymer

Description description	ATP synthase subunit b
Molecular weight formula_weight	19437.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,L,N

MGEAAHGISGGTIIYQLLMFIILLALLRKFAWQPLMNIMKQREEHIANEIDQAEKRRQEAEKLLEEQRELMKQSRQEAQALIENARKLAEEQKEQIVASARAEAERVKETAKKEIEREKEQAMAALREQVASLSVLIASKVIEKELTEQDQRKLIEAYIKDVQEVGGAR

Source Source

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

Entity 7 Entity 7 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	4

▶

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	triclinic

Resolution resolution	2.79 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	88259

Engineering of ATP synthase

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

ATP synthase subunit beta

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 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 delta subunit,ATP synthase subunit alpha,ATP synthase subunit alpha

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

9jc1__assembly_1__model_1

9jc1__assembly_1__model_1 | I(q)

9jc1__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 (8)

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

Entity 6 Entity 6 polymer

Polymer Polymer

Source Source

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

7. Citations (1)