1c17

A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE

Method: SOLUTION NMR

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

ATP SYNTHASE SUBUNIT C

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 13	ATP SYNTHASE SUBUNIT A × 1 （P0AB98）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPL_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–79； UniProt 1–79 Author chain B； PDBConstruct 1–79； UniProt 1–79 Author chain C； PDBConstruct 1–79； UniProt 1–79 Author chain D； PDBConstruct 1–79； UniProt 1–79 Author chain E； PDBConstruct 1–79； UniProt 1–79 Author chain F； PDBConstruct 1–79； UniProt 1–79 Author chain G； PDBConstruct 1–79； UniProt 1–79 Author chain H； PDBConstruct 1–79； UniProt 1–79 Author chain I； PDBConstruct 1–79； UniProt 1–79 Author chain J； PDBConstruct 1–79； UniProt 1–79 Author chain K； PDBConstruct 1–79； UniProt 1–79 Author chain L； PDBConstruct 1–79； UniProt 1–79

ATP SYNTHASE SUBUNIT A

Escherichia coli

UniProt P0AB98

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 13	ATP SYNTHASE SUBUNIT C × 12 （P68699）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATP6_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain M； PDBConstruct 1–177； UniProt 95–271

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	1c17
Deposition date deposition_date	1999-07-20
Structure title title	A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE
Keywords keywords	MEMBRANE PROTEIN, HELIX, COMPLEX; MEMBRANE PROTEIN
Experimental Method method	SOLUTION NMR

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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.

1c17__assembly_1__model_1

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

Download this curve (.dat)

1c17__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1c17__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	32.41 Å
Rg (electron density)	31.89 Å
Total Rg	32.54 Å
Atom count	16649
Residues	1090
Excluded volume	149720 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1c17__assembly_1__model_1`	tridecameric （13）	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 (2)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE SUBUNIT C
Molecular weight formula_weight	8259.1 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L
Atom count atom_count	16649

MENLNMDLLYMAAAVMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLVDAIPMIAVGLGLYVMFAVA

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE SUBUNIT A
Molecular weight formula_weight	19869.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M

HGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHVLGLPALRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 26 domains

SCOP 2.08 (13 domains)

Domain ID domain_id	d1c17a_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17b_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17c_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17d_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17e_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17f_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17g_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17h_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17i_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17j_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17k_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17l_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.1 — Rotary ATPase ring subunits
Family Family family	f.17.1.1 — F1F0 ATP synthase subunit C or V-type proton ATPase subunit c

Domain ID domain_id	d1c17m_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.18 — F1F0 ATP synthase subunit A
Superfamily Superfamily superfamily	f.18.1 — F1F0 ATP synthase subunit A
Family Family family	f.18.1.1 — F1F0 ATP synthase subunit A

CATH v4.4 (13 domains)

Domain ID domain_id	1c17A00
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	1c17B00
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	1c17C00
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	1c17D00
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	1c17E00
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	1c17F00
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	1c17G00
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	1c17H00
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	1c17I00
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	1c17J00
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	1c17K00
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	1c17L00
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	1c17M00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	220 — ATP synthase, F0 complex, subunit A

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE

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

ATP SYNTHASE SUBUNIT C

State in the Current Structure

Other States of the Same Protein in the Database

ATP SYNTHASE SUBUNIT A

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

1c17__assembly_1__model_1

1c17__assembly_1__model_1 | I(q)

1c17__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 26 domains

SCOP 2.08 (13 domains)

CATH v4.4 (13 domains)

7. Citations (1)

A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE

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

ATP SYNTHASE SUBUNIT C

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 A

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

1c17__assembly_1__model_1

1c17__assembly_1__model_1 | I(q)

1c17__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 26 domains

SCOP 2.08 (13 domains)

CATH v4.4 (13 domains)

7. Citations (1)