SAXSdb — 1a91

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

F1FO ATPASE SUBUNIT C

Escherichia coli

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–79	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5；300 K	Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1A91	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ATY DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE 2D NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C OF THE F1FO ATP SYNTHASE Deposited 1994-10-05	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–79（79 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1C0V SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES Deposited 1999-07-22	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–79（79 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；300 K；Pressure 1 NMR sample composition 4:4:1	Resolution not provided
1C17 A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE Deposited 1999-07-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric	Chain A 1–79（79 aa） Chain B 1–79（79 aa） Chain C 1–79（79 aa） Chain D 1–79（79 aa） Chain E 1–79（79 aa） Chain F 1–79（79 aa） Chain G 1–79（79 aa） Chain H 1–79（79 aa） Chain I 1–79（79 aa） Chain J 1–79（79 aa） Chain K 1–79（79 aa） Chain L 1–79（79 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM；Pressure AMBIENT NMR measurement conditions pH 8；300 K；Ionic strength (raw mmCIF value) 50 mM；Pressure AMBIENT NMR sample composition 1 MM SUBUNIT C	Resolution not provided
1C99 ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI Deposited 1999-04-30	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–79（79 aa） Fragment：subunit c	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 8；300 K	Resolution not provided
1IJP Solution Structure of Ala20Pro/Pro64Ala substituted subunit c of Escherichia coli ATP synthase Deposited 2001-04-27	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–79（79 aa） Fragment：subunit c	Mutation：A20P, P64A	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM NaCl；Pressure atmospheric NMR sample composition 2.2 mM subunit c, 50 mM NaCl, pH 5.0 \| CDCl3:CD3OD:D2O=4:4:1 or CDCl3:CD3OH:H2O=4:4:1	Resolution not provided
1L6T STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE Deposited 2002-03-13	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–79（79 aa）	Mutation：A24D, D61N	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；300 K；Ionic strength (raw mmCIF value) 50 mM NACL；Pressure ATMOSPHERIC NMR sample composition 2.0 MM SUBUNIT C, 50 MM NACL, PH 5.0 \| CDCl3:CD3OH:H20=4:4:1	Resolution not provided
4UTQ A structural model of the active ribosome-bound membrane protein insertase YidC Deposited 2014-07-22	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Z 1–79（79 aa） Fragment：MEMBRANE DOMAIN	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- FEI VITROBOT MARK IV,	Resolution 8.00 Å

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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

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	1a91
Deposition date deposition_date	1998-04-15
Structure title title	SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES
Keywords keywords	MEMBRANE PROTEIN, HYDROGEN ION TRANSPORT; MEMBRANE PROTEIN
Experimental Method method	SOLUTION NMR

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	18.00 Å
Radius of gyration Rg (electron density) rg_electron	18.39 Å
Forward intensity I(0) i0	78086000.00
Molecular weight molecular_weight	82541.0 kDa
Excluded volume excluded_volume	107030 Å³
Envelope volume envelope_volume	20496 Å³
Hydration-shell volume shell_volume	9987 Å³
Envelope diameter envelope_diameter	68.1 Å
Shell Rg shell_rg	23.53 Å
Envelope Rg envelope_rg	20.64 Å
Shape Rg shape_rg	18.35 Å
Total Rg total_rg	18.76 Å
Total atoms total_atoms	11910
Residues n_residues	790
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	66.2 Å
Rg (real space) rg_real	18.57 Å
Rg uncertainty (real space) rg_real_error	0.94 Å
I(0) (real space) i0_real	7.8090e+07
I(0) uncertainty (real space) i0_real_error	1.1050e+06
Rg (reciprocal space) rg_reciprocal	18.50 Å
I(0) (reciprocal space) i0_reciprocal	78080000.0000
Solution quality estimate total_estimate	0.6524
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	10.7 Å
Skewness Skewness skewness	0.590
Kurtosis Kurtosis kurtosis	-0.608
Angular range angular_range	— – 0.4400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	42420.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.161; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.009; Smooth: 0.990

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1a91a_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1a91A00
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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8. Citations (2)

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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	—

Description description	F1FO ATPASE SUBUNIT C
Molecular weight formula_weight	8259.1 kDa
EC 编号 ec_number	3.6.1.34
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	11910

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI; NMR, 10 STRUCTURES

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

F1FO ATPASE SUBUNIT C

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/a9/1a91/1a91.fit
pddf	/app/data/pr_computation/a9/1a91/1a91.pr.out
profile	/app/data/saxs_computation/a9/1a91/1a91.dat