4cbj

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

Method: X-RAY DIFFRACTION

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

ATP SYNTHASE SUBUNIT C

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 13	dodecyl 2-(trimethylammonio)ethyl phosphate × 13 TRIS(HYDROXYETHYL)AMINOMETHANE × 3 DODECYL-BETA-D-MALTOSIDE × 1 water × 10	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ATPL_BACPE
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–69； UniProt 1–69 Author chain B； PDBConstruct 1–69； UniProt 1–69 Author chain I； PDBConstruct 1–69； UniProt 1–69 Author chain J； PDBConstruct 1–69； UniProt 1–69 Author chain K； PDBConstruct 1–69； UniProt 1–69 Author chain L； PDBConstruct 1–69； UniProt 1–69 Author chain M； PDBConstruct 1–69； UniProt 1–69 Author chain C； PDBConstruct 1–69； UniProt 1–69 Author chain D； PDBConstruct 1–69； UniProt 1–69 Author chain E； PDBConstruct 1–69； UniProt 1–69 Author chain F； PDBConstruct 1–69； UniProt 1–69 Author chain G； PDBConstruct 1–69； UniProt 1–69 Author chain H； PDBConstruct 1–69； UniProt 1–69

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	4cbj
Deposition date deposition_date	2013-10-14
Structure title title	The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology
Keywords keywords	F1FO-ATP SYNTHASE, C-RING ROTOR, ION BINDING POCKET, TRANSFERASE; TRANSFERASE
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.

4cbj__assembly_1__model_1

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

Download this curve (.dat)

4cbj__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4cbj__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.12 Å
Rg (electron density)	26.78 Å
Total Rg	27.59 Å
Atom count	6712
Residues	890
Excluded volume	127140 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4cbj__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 (6)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE SUBUNIT C
Molecular weight formula_weight	6961.4 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,I,J,K,L,M
Atom count atom_count	6732

MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRGTLQTLMFIGVALAEAVPIIAIVISLLILF

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE SUBUNIT C
Molecular weight formula_weight	6933.4 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

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

MAFLGAAIAAGLAAVAGAIAVAIIVKATIEGTTRQPELRGTLQTLMFIGVALAEAVPIIAIVISLLILF

Entity 3 Entity 3 non-polymer

Description description	dodecyl 2-(trimethylammonio)ethyl phosphate
Molecular weight formula_weight	351.5 kDa
Source method src_method	syn
Copy count entity_count	13

Entity 4 Entity 4 non-polymer

Description description	TRIS(HYDROXYETHYL)AMINOMETHANE
Molecular weight formula_weight	163.2 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	DODECYL-BETA-D-MALTOSIDE
Molecular weight formula_weight	510.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	20

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6. Fold Classification (SCOP + CATH) 13 domains

CATH v4.4 (13 domains)

Domain ID domain_id	4cbjA00
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	4cbjB00
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	4cbjC00
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	4cbjD00
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	4cbjE00
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	4cbjF00
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	4cbjG00
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	4cbjH00
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	4cbjI00
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	4cbjJ00
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	4cbjK00
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	4cbjL00
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	4cbjM00
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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Unit-cell length a length_a	73.940 Å
Unit-cell length b length_b	98.330 Å
Unit-cell length c length_c	121.930 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.28 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	14

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	48.332 Å
R factor r_factor	0.2376
R_work r_work	0.2351
R_free r_free	0.2878

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4cbj__assembly_1__model_1

4cbj__assembly_1__model_1 | I(q)

4cbj__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 13 domains

CATH v4.4 (13 domains)

7. Citations (1)

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4cbj__assembly_1__model_1

4cbj__assembly_1__model_1 | I(q)

4cbj__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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 13 domains

CATH v4.4 (13 domains)

7. Citations (1)