2w6j

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 5.

Method: X-RAY DIFFRACTION

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

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL

OrganismNot specified

UniProt P19483

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 9	ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00829） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P05631） F1-ATPASE DELTA SUBUNIT × 1 （P05630） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P05632）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPA1_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–553； UniProt 1–553 Author chain B； PDBConstruct 1–553； UniProt 1–553 Author chain C； PDBConstruct 1–553； UniProt 1–553

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00829

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 9	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 （P19483） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P05631） F1-ATPASE DELTA SUBUNIT × 1 （P05630） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P05632）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPB_BOVIN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–528； UniProt 1–528 Author chain E； PDBConstruct 1–528； UniProt 1–528 Author chain F； PDBConstruct 1–528； UniProt 1–528

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P05631

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 9	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 （P19483） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00829） F1-ATPASE DELTA SUBUNIT × 1 （P05630） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P05632）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPG_BOVIN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–298； UniProt 1–298

F1-ATPASE DELTA SUBUNIT

OrganismNot specified

UniProt P05630

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 9	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 （P19483） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00829） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P05631） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P05632）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPD_BOVIN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–168； UniProt 1–168

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P05632

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 9	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL × 3 （P19483） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00829） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P05631） F1-ATPASE DELTA SUBUNIT × 1 （P05630）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATP5E_BOVIN
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain I； PDBConstruct 1–51； UniProt 1–51

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	2w6j
Deposition date deposition_date	2008-12-18
Structure title title	Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 5.
Keywords keywords	;ATP PHOSPHORYLASE (H+ TRANSPORTING), TRANSIT PEPTIDE, F1FO ATP SYNTHASE, ATP PHOSPHORYLASE, ATP SYNTHASE, ION TRANSPORT, MITOCHONDRION, ATP SYNTHESIS, UBL CONJUGATION, CF(1), P-LOOP, HYDROLASE, NUCLEOTIDE-BINDING, HYDROGEN ION TRANSPORT, PYRROLIDONE CARBOXYLIC ACID, ATP-BINDING ;; HYDROLASE
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.

2w6j__assembly_1__model_1

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

Download this curve (.dat)

2w6j__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2w6j__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	43.77 Å
Rg (electron density)	42.96 Å
Total Rg	43.34 Å
Atom count	23874
Residues	3138
Excluded volume	427810 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2w6j__assembly_1__model_1`	nonameric （9）	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 (5)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL
Molecular weight formula_weight	59795.5 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	23874

MLSVRVAAAVARALPRRAGLVSKNALGSSFIAARNLHASNSRLQKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
Molecular weight formula_weight	56340.2 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS

Entity 3 Entity 3 polymer

Description description	ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
Molecular weight formula_weight	33119.0 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

MFSRAGVAGLSAWTVQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTHSDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Entity 4 Entity 4 polymer

Description description	F1-ATPASE DELTA SUBUNIT
Molecular weight formula_weight	17627.0 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE

Entity 5 Entity 5 polymer

Description description	ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL
Molecular weight formula_weight	5793.9 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

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6. Fold Classification (SCOP + CATH) 22 domains

CATH v4.4 (22 domains)

Domain ID domain_id	2w6jA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2w6jA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jA03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	150 — Lysin
Homologous superfamily homologous superfamily	20 — ATP synthase alpha/beta chain, C-terminal domain

Domain ID domain_id	2w6jB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2w6jB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jB03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	150 — Lysin
Homologous superfamily homologous superfamily	20 — ATP synthase alpha/beta chain, C-terminal domain

Domain ID domain_id	2w6jC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	2w6jC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jC03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	150 — Lysin
Homologous superfamily homologous superfamily	20 — ATP synthase alpha/beta chain, C-terminal domain

Domain ID domain_id	2w6jD01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	2w6jD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jD03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily	10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3

Domain ID domain_id	2w6jE01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	2w6jE02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jE03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily	10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3

Domain ID domain_id	2w6jF01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	170 —

Domain ID domain_id	2w6jF02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	2w6jF03
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1140 — Bovine Mitochondrial F1-ATPase, ATP Synthase Beta Chain; Chain D, domain3
Homologous superfamily homologous superfamily	10 — Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3

Domain ID domain_id	2w6jG01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	80 — ATP synthase, gamma subunit, helix hairpin domain

Domain ID domain_id	2w6jG02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	10 — ATP synthase, F1 complex, gamma subunit

Domain ID domain_id	2w6jH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily	10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal

Domain ID domain_id	2w6jH02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	440 — ATP synthase delta/epsilon subunit, C-terminal domain

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Unit-cell length a length_a	106.930 Å
Unit-cell length b length_b	124.070 Å
Unit-cell length c length_c	264.460 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	12

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.840 Å
Low-resolution limit resolution_low	132.450 Å
R factor r_factor	0.3050
R_work r_work	0.3050
R_free r_free	—

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 5.

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

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL

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 BETA, MITOCHONDRIAL

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 GAMMA, MITOCHONDRIAL

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

F1-ATPASE DELTA SUBUNIT

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 EPSILON, MITOCHONDRIAL

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

2w6j__assembly_1__model_1

2w6j__assembly_1__model_1 | I(q)

2w6j__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 22 domains

CATH v4.4 (22 domains)

7. Citations (1)