2wpd

The Mg.ADP inhibited state of the yeast F1c10 ATP synthase

Method: X-RAY DIFFRACTION

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

ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00830） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P38077） ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 （Q12165） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P21306） ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 10 （P61829） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPA_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–510； UniProt 36–545 Author chain B； PDBConstruct 1–510； UniProt 36–545 Author chain C； PDBConstruct 1–510； UniProt 36–545

ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL

OrganismNot specified

UniProt P00830

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 （P07251） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P38077） ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 （Q12165） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P21306） ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 10 （P61829） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPB_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–478； UniProt 34–511 Author chain E； PDBConstruct 1–478； UniProt 34–511 Author chain F； PDBConstruct 1–478； UniProt 34–511

ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL

OrganismNot specified

UniProt P38077

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 （P07251） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00830） ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 （Q12165） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P21306） ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 10 （P61829） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPG_YEAST
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–278； UniProt 34–311

ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL

OrganismNot specified

UniProt Q12165

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 （P07251） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00830） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P38077） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P21306） ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 10 （P61829） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPD_YEAST
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–138； UniProt 23–160

ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL

OrganismNot specified

UniProt P21306

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 （P07251） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00830） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P38077） ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 （Q12165） ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL × 10 （P61829） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATP5E_YEAST
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain I； PDBConstruct 1–61； UniProt 2–62

ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL

OrganismNot specified

UniProt P61829

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 19	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL × 3 （P07251） ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL × 3 （P00830） ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL × 1 （P38077） ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL × 1 （Q12165） ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL × 1 （P21306） ADENOSINE-5'-TRIPHOSPHATE × 3 MAGNESIUM ION × 5 ADENOSINE-5'-DIPHOSPHATE × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATP9_YEAST
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain J； PDBConstruct 1–76； UniProt 1–76 Author chain K； PDBConstruct 1–76； UniProt 1–76 Author chain L； PDBConstruct 1–76； UniProt 1–76 Author chain M； PDBConstruct 1–76； UniProt 1–76 Author chain N； PDBConstruct 1–76； UniProt 1–76 Author chain O； PDBConstruct 1–76； UniProt 1–76 Author chain P； PDBConstruct 1–76； UniProt 1–76 Author chain Q； PDBConstruct 1–76； UniProt 1–76 Author chain R； PDBConstruct 1–76； UniProt 1–76 Author chain S； PDBConstruct 1–76； UniProt 1–76

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	2wpd
Deposition date deposition_date	2009-08-05
Structure title title	The Mg.ADP inhibited state of the yeast F1c10 ATP synthase
Keywords keywords	;ATP PHOSPHORYLASE (H+ TRANSPORTING), ATP-BINDING, CENTRAL STALK, HYDROLASE, ATP SYNTHESIS, PHOSPHOPROTEIN, MEMBRANE PROTEIN, LIPID-BINDING, ION TRANSPORT, NUCLEOTIDE-BINDING, HYDROGEN ION TRANSPORT ;; 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.

2wpd__assembly_1__model_1

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

Download this curve (.dat)

2wpd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wpd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	57.36 Å
Rg (electron density)	59.46 Å
Total Rg	59.73 Å
Atom count	30826
Residues	4090
Excluded volume	554890 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wpd__assembly_1__model_1`	nonadecameric （19）	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 (9)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL
Molecular weight formula_weight	55007.4 kDa
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	30826

ASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL
Molecular weight formula_weight	51181.1 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

ASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN

Entity 3 Entity 3 polymer

Description description	ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL
Molecular weight formula_weight	30657.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

ATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG

Entity 4 Entity 4 polymer

Description description	ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL
Molecular weight formula_weight	14565.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

AEAAAASSGLKLQFALPHETLYSGSEVTQVNLPAKSGRIGVLANHVPTVEQLLPGVVEVMEGSNSKKFFISGGFATVQPDSQLCVTAIEAFPLESFSQENIKNLLAEAKKNVSSSDAREAAEAAIQVEVLENLQSVLK

Entity 5 Entity 5 polymer

Description description	ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL
Molecular weight formula_weight	6618.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

SAWRKAGISYAAYLNVAAQAIRSSLKTELQTASVLNRSQTDAFYTQYKNGTAASEPTPITK

Entity 6 Entity 6 polymer

Description description	ATP SYNTHASE SUBUNIT 9, MITOCHONDRIAL
Molecular weight formula_weight	7762.4 kDa
EC 编号 ec_number	3.6.3.14
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

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

MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRNPSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV

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

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6. Fold Classification (SCOP + CATH) 31 domains

CATH v4.4 (31 domains)

Domain ID domain_id	2wpdA01
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	2wpdA02
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	2wpdA03
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	2wpdB01
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	2wpdB02
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	2wpdB03
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	2wpdC01
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	2wpdC02
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	2wpdC03
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	2wpdD01
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	2wpdD02
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	2wpdD03
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	2wpdE01
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	2wpdE02
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	2wpdE03
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	2wpdF01
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	2wpdF02
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	2wpdF03
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	2wpdG01
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	2wpdG02
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	2wpdI00
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	2wpdJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdK00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdL00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdM00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdN00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdO00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdP00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdQ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdR00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

Domain ID domain_id	2wpdS00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily	10 — F1F0 ATP synthase subunit C

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7. Citations (6)

Crystal Structure of the Mg.Adp-Inhibited State of the Yeast F1C10-ATP Synthase.

J.Biol.Chem. (2010)

PMID: 20610387 · DOI: 10.1074/JBC.M110.124529 PRIMARY

Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides.

J.Biol.Chem. (2009)

PMID: 19233840 · DOI: 10.1074/JBC.M900544200

;Hydrogenated and Fluorinated Surfactants Derived from Tris(Hydroxymethyl)-Acrylamidomethane Allow the Purification of a Highly Active Yeast F1-F0 ATP-Synthase with an Enhanced Stability. ;

J.Bioenerg.Biomembr. (2009)

PMID: 19821035 · DOI: 10.1007/S10863-009-9235-5

Novel Features of the Rotary Catalytic Mechanism Revealed in the Structure of Yeast F1 ATPase.

Embo J. (2006)

PMID: 17082766 · DOI: 10.1038/SJ.EMBOJ.7601410

Structure of the Rotor Ring of F-Type Na+-ATPase from Ilyobacter Tartaricus.

Science (2005)

PMID: 15860619 · DOI: 10.1126/SCIENCE.1111199

Molecular Architecture of the Rotary Motor in ATP Synthase.

Science (1999)

PMID: 10576729 · DOI: 10.1126/SCIENCE.286.5445.1700

Unit-cell length a length_a	134.990 Å
Unit-cell length b length_b	173.944 Å
Unit-cell length c length_c	137.016 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.69 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.432 Å
Low-resolution limit resolution_low	39.775 Å
R factor r_factor	0.2868
R_work r_work	0.2863
R_free r_free	0.2972

The Mg.ADP inhibited state of the yeast F1c10 ATP synthase

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

ATP SYNTHASE SUBUNIT ALPHA, 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

ATP SYNTHASE SUBUNIT DELTA, 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 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

ATP SYNTHASE SUBUNIT 9, 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

2wpd__assembly_1__model_1

2wpd__assembly_1__model_1 | I(q)

2wpd__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 (9)

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

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

6. Fold Classification (SCOP + CATH) 31 domains

CATH v4.4 (31 domains)

7. Citations (6)