1mab

RAT LIVER F1-ATPASE

Method: X-RAY DIFFRACTION

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

PROTEIN (F1-ATPASE ALPHA CHAIN)

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	PROTEIN (F1-ATPASE BETA CHAIN) × 3 （P10719） PROTEIN (F1-ATPASE GAMMA CHAIN) × 1 （P35435） MAGNESIUM ION × 3 ADENOSINE-5'-TRIPHOSPHATE × 3 PHOSPHATE ION × 3 ADENOSINE-5'-DIPHOSPHATE × 3 water × 7	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPA_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–510； UniProt 34–543

PROTEIN (F1-ATPASE BETA CHAIN)

OrganismNot specified

UniProt P10719

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	PROTEIN (F1-ATPASE ALPHA CHAIN) × 3 （P15999） PROTEIN (F1-ATPASE GAMMA CHAIN) × 1 （P35435） MAGNESIUM ION × 3 ADENOSINE-5'-TRIPHOSPHATE × 3 PHOSPHATE ION × 3 ADENOSINE-5'-DIPHOSPHATE × 3 water × 7	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPB_RAT
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–479； UniProt 51–529

PROTEIN (F1-ATPASE GAMMA CHAIN)

OrganismNot specified

UniProt P35435

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 7	PROTEIN (F1-ATPASE ALPHA CHAIN) × 3 （P15999） PROTEIN (F1-ATPASE BETA CHAIN) × 3 （P10719） MAGNESIUM ION × 3 ADENOSINE-5'-TRIPHOSPHATE × 3 PHOSPHATE ION × 3 ADENOSINE-5'-DIPHOSPHATE × 3 water × 7	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPG_RAT
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–270； UniProt 4–273

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	1mab
Deposition date deposition_date	1998-08-06
Structure title title	RAT LIVER F1-ATPASE
Keywords keywords	ATP SYNTHASE, FOF1-ATPASE, OXIDATIVE PHOSPHORYLATION, MITOCHONDRIA, 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.

1mab__assembly_1__model_1

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

Download this curve (.dat)

1mab__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1mab__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	41.61 Å
Rg (electron density)	40.74 Å
Total Rg	41.16 Å
Atom count	22655
Residues	2962
Excluded volume	404320 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1mab__assembly_1__model_1`	heptameric （7）	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 (8)

Entity 1 Entity 1 polymer

Description description	PROTEIN (F1-ATPASE ALPHA CHAIN)
Molecular weight formula_weight	55348.2 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	A
Atom count atom_count	8489

QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRTDGKISEQSDAKLKEIVTNFLAGFEP

Entity 2 Entity 2 polymer

Description description	PROTEIN (F1-ATPASE BETA CHAIN)
Molecular weight formula_weight	51404.5 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	B

SAAPKAGTATGQIVAVIGAVVDVQFDEGLPPILNALEVQGRESRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGDYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS

Entity 3 Entity 3 polymer

Description description	PROTEIN (F1-ATPASE GAMMA CHAIN)
Molecular weight formula_weight	29974.4 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

RDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGTGSLALYEKAEIKGPEDKKKHLIIGVSSDRGLCGAIHSSVAKQMKNDMAALTAAGKEVMIVGIGEKIKSILYRTHSDQFLVSFKDVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNQFKSVISYKTEEKPIFSFSTVVAAENMSIYDDIDADVLQNYQEYNLANIIYYSLKESTTSEQSARMTAMDNASKNASDMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Entity 4 Entity 4 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

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

Entity 7 Entity 7 non-polymer

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

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	61

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6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d1maba1
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	d1maba2
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	d1maba3
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	d1mabb1
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	d1mabb2
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	d1mabb3
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	d1mabg_
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

CATH v4.4 (7 domains)

Domain ID domain_id	1mabA01
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	1mabA02
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	1mabA03
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	1mabB01
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	1mabB02
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	1mabB03
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	1mabG00
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

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Unit-cell length a length_a	143.670 Å
Unit-cell length b length_b	143.670 Å
Unit-cell length c length_c	361.150 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.2170
R_work r_work	0.2170
R_free r_free	0.2900

RAT LIVER F1-ATPASE

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

PROTEIN (F1-ATPASE ALPHA CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (F1-ATPASE BETA CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN (F1-ATPASE GAMMA CHAIN)

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1mab__assembly_1__model_1

1mab__assembly_1__model_1 | I(q)

1mab__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 (8)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

CATH v4.4 (7 domains)

7. Citations (4)

RAT LIVER F1-ATPASE

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

PROTEIN (F1-ATPASE ALPHA 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

PROTEIN (F1-ATPASE 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

PROTEIN (F1-ATPASE 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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1mab__assembly_1__model_1

1mab__assembly_1__model_1 | I(q)

1mab__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 (8)

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 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (7 domains)

CATH v4.4 (7 domains)

7. Citations (4)