2v7q

The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1.

Method: X-RAY DIFFRACTION

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

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 10	ATP SYNTHASE SUBUNIT BETA × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ATPASE INHIBITOR × 1 （P01096） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	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 1–510； UniProt 44–553 Author chain B； PDBConstruct 1–510； UniProt 44–553 Author chain C； PDBConstruct 1–510； UniProt 44–553

ATP SYNTHASE SUBUNIT BETA

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 10	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM × 3 （Q1JQC4） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ATPASE INHIBITOR × 1 （P01096） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	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 1–482； UniProt 47–528 Author chain E； PDBConstruct 1–482； UniProt 47–528 Author chain F； PDBConstruct 1–482； UniProt 47–528

ATP SYNTHASE GAMMA CHAIN

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 10	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM × 3 （Q1JQC4） ATP SYNTHASE SUBUNIT BETA × 3 （P00829） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ATPASE INHIBITOR × 1 （P01096） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	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 1–272； UniProt 26–297

ATP SYNTHASE DELTA CHAIN

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 10	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM × 3 （Q1JQC4） ATP SYNTHASE SUBUNIT BETA × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ATPASE INHIBITOR × 1 （P01096） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	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 1–146； UniProt 23–168

ATP SYNTHASE EPSILON CHAIN

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 10	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM × 3 （Q1JQC4） ATP SYNTHASE SUBUNIT BETA × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATPASE INHIBITOR × 1 （P01096） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	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 1–50； UniProt 1–50

ATPASE INHIBITOR

BOS TAURUS

UniProt P01096

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 10	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM × 3 （Q1JQC4） ATP SYNTHASE SUBUNIT BETA × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2 PHOSPHATE ION × 1 water × 10	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATIF1_BOVIN
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain J； PDBConstruct 1–60； UniProt 26–85

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	2v7q
Deposition date deposition_date	2007-07-31
Structure title title	The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1.
Keywords keywords	ION TRANSPORT, MITOCHONDRION, TRANSIT PEPTIDE, INHIBITOR PROTEIN, HYDROLASE; 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.

2v7q__assembly_1__model_1

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

Download this curve (.dat)

2v7q__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2v7q__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	44.83 Å
Rg (electron density)	44.14 Å
Total Rg	44.44 Å
Atom count	25478
Residues	3323
Excluded volume	455600 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2v7q__assembly_1__model_1`	decameric （10）	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 (11)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM
Molecular weight formula_weight	55332.2 kDa
EC 编号 ec_number	3.6.1.14
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	27418

EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE SUBUNIT BETA
Molecular weight formula_weight	51757.8 kDa
EC 编号 ec_number	3.6.1.14
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

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

AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS

Entity 3 Entity 3 polymer

Description description	ATP SYNTHASE GAMMA CHAIN
Molecular weight formula_weight	30185.7 kDa
EC 编号 ec_number	3.6.1.34
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTHSDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Entity 4 Entity 4 polymer

Description description	ATP SYNTHASE DELTA CHAIN
Molecular weight formula_weight	15074.8 kDa
EC 编号 ec_number	3.6.1.14
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE

Entity 5 Entity 5 polymer

Description description	ATP SYNTHASE EPSILON CHAIN
Molecular weight formula_weight	5662.7 kDa
EC 编号 ec_number	3.6.1.14
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Entity 6 Entity 6 polymer

Description description	ATPASE INHIBITOR
Molecular weight formula_weight	7462.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIHHHHHH

Source Source

Source organism organism	BOS TAURUS
Common name common_name	COW
NCBI taxonomy ID ncbi_taxonomy_id	9913
Host organism host_organism	ESCHERICHIA COLI

Entity 7 Entity 7 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	3

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	5

Entity 9 Entity 9 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 10 Entity 10 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1940

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6. Fold Classification (SCOP + CATH) 47 domains

SCOP 2.08 (23 domains)

Domain ID domain_id	d2v7qa1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.0 — automated matches

Domain ID domain_id	d2v7qa2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qa3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.0 — automated matches

Domain ID domain_id	d2v7qb1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.0 — automated matches

Domain ID domain_id	d2v7qb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qb3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.0 — automated matches

Domain ID domain_id	d2v7qc1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.0 — automated matches

Domain ID domain_id	d2v7qc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qc3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.0 — automated matches

Domain ID domain_id	d2v7qd1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qd2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qd3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qe1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qe2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qe3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qf1
Class class	b — All beta proteins
Fold Fold fold	b.49 — Domain of alpha and beta subunits of F1 ATP synthase-like
Superfamily Superfamily superfamily	b.49.1 — N-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	b.49.1.1 — N-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qf2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.11 — RecA protein-like (ATPase-domain)

Domain ID domain_id	d2v7qf3
Class class	a — All alpha proteins
Fold Fold fold	a.69 — Left-handed superhelix
Superfamily Superfamily superfamily	a.69.1 — C-terminal domain of alpha and beta (or A/B) subunits of rotary ATPases
Family Family family	a.69.1.1 — C-terminal domain of alpha and beta subunits of F1 ATP synthase

Domain ID domain_id	d2v7qg_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.2 — ATP synthase (F1-ATPase), gamma subunit
Family Family family	c.49.2.1 — ATP synthase (F1-ATPase), gamma subunit

Domain ID domain_id	d2v7qh1
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family family	a.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain

Domain ID domain_id	d2v7qh2
Class class	b — All beta proteins
Fold Fold fold	b.93 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Superfamily Superfamily superfamily	b.93.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Family Family family	b.93.1.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain

Domain ID domain_id	d2v7qi_
Class class	a — All alpha proteins
Fold Fold fold	a.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamily	a.137.8 — Epsilon subunit of mitochondrial F1F0-ATP synthase
Family Family family	a.137.8.1 — Epsilon subunit of mitochondrial F1F0-ATP synthase

Domain ID domain_id	d2v7qj_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.8 — F1 ATPase inhibitor, IF1, C-terminal domain
Family Family family	h.4.8.1 — F1 ATPase inhibitor, IF1, C-terminal domain

CATH v4.4 (24 domains)

Domain ID domain_id	2v7qA01
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	2v7qA02
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	2v7qA03
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	2v7qB01
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	2v7qB02
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	2v7qB03
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	2v7qC01
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	2v7qC02
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	2v7qC03
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	2v7qD01
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	2v7qD02
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	2v7qD03
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	2v7qE01
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	2v7qE02
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	2v7qE03
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	2v7qF01
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	2v7qF02
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	2v7qF03
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	2v7qG01
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	2v7qG02
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	2v7qH01
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	2v7qH02
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

Domain ID domain_id	2v7qI00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1620 — Atp Synthase Epsilon Chain; Chain: I;
Homologous superfamily homologous superfamily	20 — ATP synthase, F1 complex, epsilon subunit superfamily, mitochondrial

Domain ID domain_id	2v7qJ00
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	500 — Single helix bin

▶

Unit-cell length a length_a	262.534 Å
Unit-cell length b length_b	103.271 Å
Unit-cell length c length_c	135.559 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	2.100 Å
Low-resolution limit resolution_low	37.190 Å
R factor r_factor	0.1930
R_work r_work	0.1900
R_free r_free	0.2450

The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1.

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

ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM

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

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 DELTA 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

ATPASE INHIBITOR

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

2v7q__assembly_1__model_1

2v7q__assembly_1__model_1 | I(q)

2v7q__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 (11)

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

Entity 6 Entity 6 polymer

Polymer Polymer

Source Source

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

Entity 11 Entity 11 water

6. Fold Classification (SCOP + CATH) 47 domains