SAXSdb — 9yds

▼

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

Lipoprotein

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 116	FlgO domain-containing protein × 58 （Q9KQ00）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KQ01_VIBCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain Aa； PDBConstruct 1–104； UniProt 26–130 Author chain Ac； PDBConstruct 1–104； UniProt 26–130 Author chain Ae； PDBConstruct 1–104； UniProt 26–130 Author chain Ag； PDBConstruct 1–104； UniProt 26–130 Author chain Ai； PDBConstruct 1–104； UniProt 26–130 Author chain Ak； PDBConstruct 1–104； UniProt 26–130 Author chain Am； PDBConstruct 1–104； UniProt 26–130 Author chain Ao； PDBConstruct 1–104； UniProt 26–130 Author chain Aq； PDBConstruct 1–104； UniProt 26–130 Author chain As； PDBConstruct 1–104； UniProt 26–130 Author chain Au； PDBConstruct 1–104； UniProt 26–130 Author chain Aw； PDBConstruct 1–104； UniProt 26–130 Author chain Ay； PDBConstruct 1–104； UniProt 26–130 Author chain Ba； PDBConstruct 1–104； UniProt 26–130 Author chain Bc； PDBConstruct 1–104； UniProt 26–130 Author chain Be； PDBConstruct 1–104； UniProt 26–130 Author chain Bg； PDBConstruct 1–104； UniProt 26–130 Author chain Bi； PDBConstruct 1–104； UniProt 26–130 Author chain Bk； PDBConstruct 1–104； UniProt 26–130 Author chain Bm； PDBConstruct 1–104； UniProt 26–130 Author chain Bo； PDBConstruct 1–104； UniProt 26–130 Author chain Bq； PDBConstruct 1–104； UniProt 26–130 Author chain Bs； PDBConstruct 1–104； UniProt 26–130 Author chain Bu； PDBConstruct 1–104； UniProt 26–130 Author chain Bw； PDBConstruct 1–104； UniProt 26–130 Author chain By； PDBConstruct 1–104； UniProt 26–130 Author chain Ca； PDBConstruct 1–104； UniProt 26–130 Author chain Cc； PDBConstruct 1–104； UniProt 26–130 Author chain Ce； PDBConstruct 1–104； UniProt 26–130 Author chain Cg； PDBConstruct 1–104； UniProt 26–130 Author chain Ci； PDBConstruct 1–104； UniProt 26–130 Author chain Ck； PDBConstruct 1–104； UniProt 26–130 Author chain Cm； PDBConstruct 1–104； UniProt 26–130 Author chain Co； PDBConstruct 1–104； UniProt 26–130 Author chain Cq； PDBConstruct 1–104； UniProt 26–130 Author chain Cs； PDBConstruct 1–104； UniProt 26–130 Author chain Cu； PDBConstruct 1–104； UniProt 26–130 Author chain Cw； PDBConstruct 1–104； UniProt 26–130 Author chain Cy； PDBConstruct 1–104； UniProt 26–130 Author chain Da； PDBConstruct 1–104； UniProt 26–130 Author chain Dc； PDBConstruct 1–104； UniProt 26–130 Author chain De； PDBConstruct 1–104； UniProt 26–130 Author chain Dg； PDBConstruct 1–104； UniProt 26–130 Author chain Di； PDBConstruct 1–104； UniProt 26–130 Author chain Dk； PDBConstruct 1–104； UniProt 26–130 Author chain Dm； PDBConstruct 1–104； UniProt 26–130 Author chain Do； PDBConstruct 1–104； UniProt 26–130 Author chain Dq； PDBConstruct 1–104； UniProt 26–130 Author chain Ds； PDBConstruct 1–104； UniProt 26–130 Author chain Du； PDBConstruct 1–104； UniProt 26–130 Author chain Dw； PDBConstruct 1–104； UniProt 26–130 Author chain Dy； PDBConstruct 1–104； UniProt 26–130 Author chain Ea； PDBConstruct 1–104； UniProt 26–130 Author chain Ec； PDBConstruct 1–104； UniProt 26–130 Author chain Ee； PDBConstruct 1–104； UniProt 26–130 Author chain Eg； PDBConstruct 1–104； UniProt 26–130 Author chain Ei； PDBConstruct 1–104； UniProt 26–130 Author chain Ek； PDBConstruct 1–104； UniProt 26–130

FlgO domain-containing protein

OrganismNot specified

UniProt Q9KQ00

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 116	Lipoprotein × 58 （Q9KQ01）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KQ00_VIBCH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain Ab； PDBConstruct 1–192； UniProt 30–221 Author chain Ad； PDBConstruct 1–192； UniProt 30–221 Author chain Af； PDBConstruct 1–192； UniProt 30–221 Author chain Ah； PDBConstruct 1–192； UniProt 30–221 Author chain Aj； PDBConstruct 1–192； UniProt 30–221 Author chain Al； PDBConstruct 1–192； UniProt 30–221 Author chain An； PDBConstruct 1–192； UniProt 30–221 Author chain Ap； PDBConstruct 1–192； UniProt 30–221 Author chain Ar； PDBConstruct 1–192； UniProt 30–221 Author chain At； PDBConstruct 1–192； UniProt 30–221 Author chain Av； PDBConstruct 1–192； UniProt 30–221 Author chain Ax； PDBConstruct 1–192； UniProt 30–221 Author chain Az； PDBConstruct 1–192； UniProt 30–221 Author chain Bb； PDBConstruct 1–192； UniProt 30–221 Author chain Bd； PDBConstruct 1–192； UniProt 30–221 Author chain Bf； PDBConstruct 1–192； UniProt 30–221 Author chain Bh； PDBConstruct 1–192； UniProt 30–221 Author chain Bj； PDBConstruct 1–192； UniProt 30–221 Author chain Bl； PDBConstruct 1–192； UniProt 30–221 Author chain Bn； PDBConstruct 1–192； UniProt 30–221 Author chain Bp； PDBConstruct 1–192； UniProt 30–221 Author chain Br； PDBConstruct 1–192； UniProt 30–221 Author chain Bt； PDBConstruct 1–192； UniProt 30–221 Author chain Bv； PDBConstruct 1–192； UniProt 30–221 Author chain Bx； PDBConstruct 1–192； UniProt 30–221 Author chain Bz； PDBConstruct 1–192； UniProt 30–221 Author chain Cb； PDBConstruct 1–192； UniProt 30–221 Author chain Cd； PDBConstruct 1–192； UniProt 30–221 Author chain Cf； PDBConstruct 1–192； UniProt 30–221 Author chain Ch； PDBConstruct 1–192； UniProt 30–221 Author chain Cj； PDBConstruct 1–192； UniProt 30–221 Author chain Cl； PDBConstruct 1–192； UniProt 30–221 Author chain Cn； PDBConstruct 1–192； UniProt 30–221 Author chain Cp； PDBConstruct 1–192； UniProt 30–221 Author chain Cr； PDBConstruct 1–192； UniProt 30–221 Author chain Ct； PDBConstruct 1–192； UniProt 30–221 Author chain Cv； PDBConstruct 1–192； UniProt 30–221 Author chain Cx； PDBConstruct 1–192； UniProt 30–221 Author chain Cz； PDBConstruct 1–192； UniProt 30–221 Author chain Db； PDBConstruct 1–192； UniProt 30–221 Author chain Dd； PDBConstruct 1–192； UniProt 30–221 Author chain Df； PDBConstruct 1–192； UniProt 30–221 Author chain Dh； PDBConstruct 1–192； UniProt 30–221 Author chain Dj； PDBConstruct 1–192； UniProt 30–221 Author chain Dl； PDBConstruct 1–192； UniProt 30–221 Author chain Dn； PDBConstruct 1–192； UniProt 30–221 Author chain Dp； PDBConstruct 1–192； UniProt 30–221 Author chain Dr； PDBConstruct 1–192； UniProt 30–221 Author chain Dt； PDBConstruct 1–192； UniProt 30–221 Author chain Dv； PDBConstruct 1–192； UniProt 30–221 Author chain Dx； PDBConstruct 1–192； UniProt 30–221 Author chain Dz； PDBConstruct 1–192； UniProt 30–221 Author chain Eb； PDBConstruct 1–192； UniProt 30–221 Author chain Ed； PDBConstruct 1–192； UniProt 30–221 Author chain Ef； PDBConstruct 1–192； UniProt 30–221 Author chain Eh； PDBConstruct 1–192； UniProt 30–221 Author chain Ej； PDBConstruct 1–192； UniProt 30–221 Author chain El； PDBConstruct 1–192； UniProt 30–221

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9yds
Deposition date deposition_date	2025-09-23
Structure title title	H-ring subunit FlgO and FlgP in Vibrio cholerae at assembled, opened state
Keywords keywords	In situ cryo-EM, sheathed flagellar motor, Vibrio cholerae, H-ring, assembled state, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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.

9yds__assembly_1__model_1

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

Download this curve (.dat)

9yds__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9yds__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	0.00 Å
Rg (electron density)	187.90 Å
Total Rg	187.90 Å
Atom count	133980
Residues	17052
Excluded volume	2360600 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9yds__assembly_1__model_1`	116-meric （116）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Lipoprotein
Molecular weight formula_weight	11848.3 kDa
Source method src_method	nat
Copy count entity_count	58

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;Aa,Ac,Ae,Ag,Ai,Ak,Am,Ao,Aq,As,Au,Aw,Ay,Ba,Bc,Be,Bg,Bi,Bk,Bm,Bo,Bq,Bs,Bu,Bw,By,Ca,Cc,Ce,Cg,Ci,Ck,Cm,Co,Cq,Cs,Cu,Cw,Cy,Da,Dc,De,Dg,Di,Dk,Dm,Do,Dq,Ds,Du,Dw,Dy,Ea,Ec,Ee,Eg,Ei,Ek ;
Atom count atom_count	133980

PDDWLTAVGYANISEQRGRDEAEKQVRAMRASKIDAYRELAEQVYGMRISGRAELQDQRLGTELTAGADGVIRGAEVVRSYKVGDSYVTELRLDIRKMDKMRDY

Entity 2 Entity 2 polymer

Description description	FlgO domain-containing protein
Molecular weight formula_weight	21563.3 kDa
Source method src_method	nat
Copy count entity_count	58

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;Ab,Ad,Af,Ah,Aj,Al,An,Ap,Ar,At,Av,Ax,Az,Bb,Bd,Bf,Bh,Bj,Bl,Bn,Bp,Br,Bt,Bv,Bx,Bz,Cb,Cd,Cf,Ch,Cj,Cl,Cn,Cp,Cr,Ct,Cv,Cx,Cz,Db,Dd,Df,Dh,Dj,Dl,Dn,Dp,Dr,Dt,Dv,Dx,Dz,Eb,Ed,Ef,Eh,Ej,El ;

APIYNGKEPYNGSQFMLMESPRHTLDFFVESMTEDLMLSNTSITARTPIAVTSFVDLQNMDTTNWLGNSVSEGFIHQFQRRGFKVVDFKTTGSIQVTQQGDFAFSRDWKNLSSEQEVQYVLTGTMLRQEGGVIVNARVVGMHSRIVVATAQGFLPADRIGRDLDTLNSIRTQDGVLIRSDPTITQPYTVILR

▶

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	triclinic

Resolution resolution	3.45 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	35317

H-ring subunit FlgO and FlgP in Vibrio cholerae at assembled, opened state

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

Lipoprotein

State in the Current Structure

Other States of the Same Protein in the Database

FlgO domain-containing 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

9yds__assembly_1__model_1

9yds__assembly_1__model_1 | I(q)

9yds__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

7. Citations (1)

H-ring subunit FlgO and FlgP in Vibrio cholerae at assembled, opened state

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

Lipoprotein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FlgO domain-containing 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

9yds__assembly_1__model_1

9yds__assembly_1__model_1 | I(q)

9yds__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

7. Citations (1)