1e79

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)

Method: X-RAY DIFFRACTION

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

ATP SYNTHASE ALPHA CHAIN HEART ISOFORM

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 BETA CHAIN × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 3 GLYCEROL × 1 DICYCLOHEXYLUREA × 1 SULFATE ION × 1 water × 9	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATP0_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 BETA CHAIN

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 ALPHA CHAIN HEART ISOFORM × 3 （P19483） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 3 GLYCEROL × 1 DICYCLOHEXYLUREA × 1 SULFATE ION × 1 water × 9	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 9	ATP SYNTHASE ALPHA CHAIN HEART ISOFORM × 3 （P19483） ATP SYNTHASE BETA CHAIN × 3 （P00829） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 3 GLYCEROL × 1 DICYCLOHEXYLUREA × 1 SULFATE ION × 1 water × 9	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 9	ATP SYNTHASE ALPHA CHAIN HEART ISOFORM × 3 （P19483） ATP SYNTHASE BETA CHAIN × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE EPSILON CHAIN × 1 （P05632） ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 3 GLYCEROL × 1 DICYCLOHEXYLUREA × 1 SULFATE ION × 1 water × 9	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 9	ATP SYNTHASE ALPHA CHAIN HEART ISOFORM × 3 （P19483） ATP SYNTHASE BETA CHAIN × 3 （P00829） ATP SYNTHASE GAMMA CHAIN × 1 （P05631） ATP SYNTHASE DELTA CHAIN × 1 （P05630） ADENOSINE-5'-TRIPHOSPHATE × 2 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 3 GLYCEROL × 1 DICYCLOHEXYLUREA × 1 SULFATE ION × 1 water × 9	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPE_BOVIN
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain I； PDBConstruct 1–50； UniProt 1–50

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	1e79
Deposition date deposition_date	2000-08-25
Structure title title	Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)
Keywords keywords	ATP PHOSPHORYLASE, ATP PHOSPHORYLASE (H+ TRANSPORTING), F1FO ATP SYNTHASE, CENTRAL STALK, 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.

1e79__assembly_1__model_1

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

Download this curve (.dat)

1e79__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1e79__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	45.26 Å
Rg (electron density)	44.57 Å
Total Rg	44.85 Å
Atom count	25407
Residues	3316
Excluded volume	454440 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1e79__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 (12)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE ALPHA CHAIN HEART ISOFORM
Molecular weight formula_weight	55301.2 kDa
EC 编号 ec_number	3.6.1.34
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	26318

QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE BETA CHAIN
Molecular weight formula_weight	51757.8 kDa
EC 编号 ec_number	3.6.1.34
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	3.6.1.34
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	3.6.1.34
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 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 8 Entity 8 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 9 Entity 9 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 non-polymer

Description description	DICYCLOHEXYLUREA
Molecular weight formula_weight	224.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 12 Entity 12 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	911

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6. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (22 domains)

Domain ID domain_id	d1e79a1
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	d1e79a2
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	d1e79a3
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	d1e79b1
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	d1e79b2
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	d1e79b3
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	d1e79c1
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	d1e79c2
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	d1e79c3
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	d1e79d1
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	d1e79d2
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	d1e79d3
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	d1e79e1
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	d1e79e2
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	d1e79e3
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	d1e79f1
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	d1e79f2
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	d1e79f3
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	d1e79g_
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	d1e79h1
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	d1e79h2
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	d1e79i_
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

CATH v4.4 (23 domains)

Domain ID domain_id	1e79A01
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	1e79A02
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	1e79A03
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	1e79B01
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	1e79B02
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	1e79B03
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	1e79C01
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	1e79C02
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	1e79C03
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	1e79D01
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	1e79D02
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	1e79D03
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	1e79E01
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	1e79E02
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	1e79E03
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	1e79F01
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	1e79F02
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	1e79F03
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	1e79G01
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	1e79G02
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	1e79H01
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	1e79H02
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	1e79I00
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

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7. Citations (7)

The Structure of the Central Stalk in Bovine F(1)-ATPase at 2.4 A Resolution.

Nat.Struct.Biol. (2000)

PMID: 11062563 · DOI: 10.1038/80981 PRIMARY

Molecular Architecture of the Rotary Motor in ATP Synthase

Science (1999)

PMID: 10576729 · DOI: 10.1126/SCIENCE.286.5445.1700

ATP Synthesis by Rotary Catalysis (Nobel Lecture)

Angew.Chem.Int.Ed.Engl. (1998)

DOI: 10.1002/(SICI)1521-3773(19980918)37:17<2308::AID-ANIE2308>3.0.CO;2-W

Crystal Structure of the Epsilon Subunit of the Proton-Translocating ATP Synthase from Escherichia Coli

Structure (1997)

PMID: 9331422 · DOI: 10.1016/S0969-2126(97)00272-4

Structure at 2.8 A Resolution of F1-ATPase from Bovine Heart Mitochondria

Nature (1994)

PMID: 8065448 · DOI: 10.1038/370621A0

Crystallization of F1-ATPase from Bovine Heart Mitochondria

J.Mol.Biol. (1993)

PMID: 8433373 · DOI: 10.1006/JMBI.1993.1081

;Inactivation of Bovine Mitochondrial F1-ATPase with Dicyclohexyl-Carbodiimide [14C] Leads to the Modification of a Specific Glutamic-Acid Residue in the Beta Subunit ;

J.Biol.Chem. (1981)

PMID: 6114957

Unit-cell length a length_a	267.200 Å
Unit-cell length b length_b	107.200 Å
Unit-cell length c length_c	135.900 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	2.400 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.2250
R_free r_free	0.2810

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)

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

ATP SYNTHASE ALPHA CHAIN 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 BETA 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 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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1e79__assembly_1__model_1

1e79__assembly_1__model_1 | I(q)

1e79__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 (12)

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 non-polymer

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 non-polymer

Entity 12 Entity 12 water

6. Fold Classification (SCOP + CATH) 45 domains

SCOP 2.08 (22 domains)

CATH v4.4 (23 domains)

7. Citations (7)