SAXSdb — 7cbl

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

Flagellar L-ring protein

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 52	Flagellar P-ring protein × 26 （P15930） OCTANOIC ACID (CAPRYLIC ACID) × 26	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FLGH_SALTY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–232； UniProt 1–232 Author chain B； PDBConstruct 1–232； UniProt 1–232 Author chain C； PDBConstruct 1–232； UniProt 1–232 Author chain D； PDBConstruct 1–232； UniProt 1–232 Author chain E； PDBConstruct 1–232； UniProt 1–232 Author chain F； PDBConstruct 1–232； UniProt 1–232 Author chain G； PDBConstruct 1–232； UniProt 1–232 Author chain H； PDBConstruct 1–232； UniProt 1–232 Author chain I； PDBConstruct 1–232； UniProt 1–232 Author chain J； PDBConstruct 1–232； UniProt 1–232 Author chain K； PDBConstruct 1–232； UniProt 1–232 Author chain L； PDBConstruct 1–232； UniProt 1–232 Author chain M； PDBConstruct 1–232； UniProt 1–232 Author chain N； PDBConstruct 1–232； UniProt 1–232 Author chain O； PDBConstruct 1–232； UniProt 1–232 Author chain P； PDBConstruct 1–232； UniProt 1–232 Author chain Q； PDBConstruct 1–232； UniProt 1–232 Author chain R； PDBConstruct 1–232； UniProt 1–232 Author chain S； PDBConstruct 1–232； UniProt 1–232 Author chain T； PDBConstruct 1–232； UniProt 1–232 Author chain U； PDBConstruct 1–232； UniProt 1–232 Author chain V； PDBConstruct 1–232； UniProt 1–232 Author chain W； PDBConstruct 1–232； UniProt 1–232 Author chain X； PDBConstruct 1–232； UniProt 1–232 Author chain Y； PDBConstruct 1–232； UniProt 1–232 Author chain Z； PDBConstruct 1–232； UniProt 1–232

Flagellar P-ring protein

OrganismNot specified

UniProt P15930

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 52	Flagellar L-ring protein × 26 （P0A1N8） OCTANOIC ACID (CAPRYLIC ACID) × 26	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FLGI_SALTY
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain a； PDBConstruct 1–365； UniProt 1–365 Author chain b； PDBConstruct 1–365； UniProt 1–365 Author chain c； PDBConstruct 1–365； UniProt 1–365 Author chain d； PDBConstruct 1–365； UniProt 1–365 Author chain e； PDBConstruct 1–365； UniProt 1–365 Author chain f； PDBConstruct 1–365； UniProt 1–365 Author chain g； PDBConstruct 1–365； UniProt 1–365 Author chain h； PDBConstruct 1–365； UniProt 1–365 Author chain i； PDBConstruct 1–365； UniProt 1–365 Author chain j； PDBConstruct 1–365； UniProt 1–365 Author chain k； PDBConstruct 1–365； UniProt 1–365 Author chain l； PDBConstruct 1–365； UniProt 1–365 Author chain m； PDBConstruct 1–365； UniProt 1–365 Author chain n； PDBConstruct 1–365； UniProt 1–365 Author chain o； PDBConstruct 1–365； UniProt 1–365 Author chain p； PDBConstruct 1–365； UniProt 1–365 Author chain q； PDBConstruct 1–365； UniProt 1–365 Author chain r； PDBConstruct 1–365； UniProt 1–365 Author chain s； PDBConstruct 1–365； UniProt 1–365 Author chain t； PDBConstruct 1–365； UniProt 1–365 Author chain u； PDBConstruct 1–365； UniProt 1–365 Author chain v； PDBConstruct 1–365； UniProt 1–365 Author chain w； PDBConstruct 1–365； UniProt 1–365 Author chain x； PDBConstruct 1–365； UniProt 1–365 Author chain y； PDBConstruct 1–365； UniProt 1–365 Author chain z； PDBConstruct 1–365； UniProt 1–365

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	7cbl
Deposition date deposition_date	2020-06-12
Structure title title	Cryo-EM structure of the flagellar LP ring from Salmonella
Keywords keywords	Flagella, LP ring, FlgH, FlgI, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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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.

7cbl__assembly_1__model_1

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

Download this curve (.dat)

7cbl__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

7cbl__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	96.63 Å
Rg (electron density)	95.52 Å
Total Rg	95.48 Å
Atom count	99242
Residues	13364
Excluded volume	1753500 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`7cbl__assembly_1__model_1`	52-meric （52）	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 (3)

Entity 1 Entity 1 polymer

Description description	Flagellar L-ring protein
Molecular weight formula_weight	24726.7 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z
Atom count atom_count	99242

MQKYALHAYPVMALMVATLTGCAWIPAKPLVQGATTAQPIPGPVPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTSFGFDTVPRYLQGLFGNSRADMEASGGNSFNGKGGANASNTFSGTLTVTVDQVLANGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNSVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM

Entity 2 Entity 2 polymer

Description description	Flagellar P-ring protein
Molecular weight formula_weight	38194.2 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p,q,r,s,t,u,v,w,x,y,z

MFKALAGIVLALVATLAHAERIRDLTSVQGVRENSLIGYGLVVGLDGTGDQTTQTPFTTQTLNNMLSQLGITVPTGTNMQLKNVAAVMVTASYPPFARQGQTIDVVVSSMGNAKSLRGGTLLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAIIERELPTQFGAGNTINLQLNDEDFTMAQQITDAINRARGYGSATALDARTVQVRVPSGNSSQVRFLADIQNMEVNVTPQDAKVVINSRTGSVVMNREVTLDSCAVAQGNLSVTVNRQLNVNQPNTPFGGGQTVVTPQTQIDLRQSGGSLQSVRSSANLNSVVRALNALGATPMDLMSILQSMQSAGCLRAKLEII

Entity 3 Entity 3 non-polymer

Description description	OCTANOIC ACID (CAPRYLIC ACID)
Molecular weight formula_weight	144.2 kDa
Source method src_method	syn
Copy count entity_count	26

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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	—

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

Resolution resolution	2.80 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	80548

Cryo-EM structure of the flagellar LP ring from Salmonella

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

Flagellar L-ring protein

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar P-ring protein

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

7cbl__assembly_1__model_1

7cbl__assembly_1__model_1 | I(q)

7cbl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)

Cryo-EM structure of the flagellar LP ring from Salmonella

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

Flagellar L-ring protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Flagellar P-ring protein

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

7cbl__assembly_1__model_1

7cbl__assembly_1__model_1 | I(q)

7cbl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

7. Citations (1)