SAXSdb — 9ydo

▼

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 156	Flagellar P-ring protein × 26 （Q9KQ14） Flagellar protein FlgT × 26 （Q9KPZ9） Sodium-type flagellar protein MotY × 26 （Q9KT95） Flagellar assembly lipoprotein FlgP × 52 （A0A2V4N6M7）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FLGH_VIBCH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain Aa； PDBConstruct 1–227； UniProt 32–258 Author chain Ab； PDBConstruct 1–227； UniProt 32–258 Author chain Ac； PDBConstruct 1–227； UniProt 32–258 Author chain Ad； PDBConstruct 1–227； UniProt 32–258 Author chain Ae； PDBConstruct 1–227； UniProt 32–258 Author chain Af； PDBConstruct 1–227； UniProt 32–258 Author chain Ag； PDBConstruct 1–227； UniProt 32–258 Author chain Ah； PDBConstruct 1–227； UniProt 32–258 Author chain Ai； PDBConstruct 1–227； UniProt 32–258 Author chain Aj； PDBConstruct 1–227； UniProt 32–258 Author chain Ak； PDBConstruct 1–227； UniProt 32–258 Author chain Al； PDBConstruct 1–227； UniProt 32–258 Author chain Am； PDBConstruct 1–227； UniProt 32–258 Author chain An； PDBConstruct 1–227； UniProt 32–258 Author chain Ao； PDBConstruct 1–227； UniProt 32–258 Author chain Ap； PDBConstruct 1–227； UniProt 32–258 Author chain Aq； PDBConstruct 1–227； UniProt 32–258 Author chain Ar； PDBConstruct 1–227； UniProt 32–258 Author chain As； PDBConstruct 1–227； UniProt 32–258 Author chain At； PDBConstruct 1–227； UniProt 32–258 Author chain Au； PDBConstruct 1–227； UniProt 32–258 Author chain Av； PDBConstruct 1–227； UniProt 32–258 Author chain Aw； PDBConstruct 1–227； UniProt 32–258 Author chain Ax； PDBConstruct 1–227； UniProt 32–258 Author chain Ay； PDBConstruct 1–227； UniProt 32–258 Author chain Az； PDBConstruct 1–227； UniProt 32–258

Flagellar P-ring protein

OrganismNot specified

UniProt Q9KQ14

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 156	Flagellar L-ring protein × 26 （Q9KQ13） Flagellar protein FlgT × 26 （Q9KPZ9） Sodium-type flagellar protein MotY × 26 （Q9KT95） Flagellar assembly lipoprotein FlgP × 52 （A0A2V4N6M7）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FLGI_VIBCH
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain Ba； PDBConstruct 1–343； UniProt 19–361 Author chain Bb； PDBConstruct 1–343； UniProt 19–361 Author chain Bc； PDBConstruct 1–343； UniProt 19–361 Author chain Bd； PDBConstruct 1–343； UniProt 19–361 Author chain Be； PDBConstruct 1–343； UniProt 19–361 Author chain Bf； PDBConstruct 1–343； UniProt 19–361 Author chain Bg； PDBConstruct 1–343； UniProt 19–361 Author chain Bh； PDBConstruct 1–343； UniProt 19–361 Author chain Bi； PDBConstruct 1–343； UniProt 19–361 Author chain Bj； PDBConstruct 1–343； UniProt 19–361 Author chain Bk； PDBConstruct 1–343； UniProt 19–361 Author chain Bl； PDBConstruct 1–343； UniProt 19–361 Author chain Bm； PDBConstruct 1–343； UniProt 19–361 Author chain Bn； PDBConstruct 1–343； UniProt 19–361 Author chain Bo； PDBConstruct 1–343； UniProt 19–361 Author chain Bp； PDBConstruct 1–343； UniProt 19–361 Author chain Bq； PDBConstruct 1–343； UniProt 19–361 Author chain Br； PDBConstruct 1–343； UniProt 19–361 Author chain Bs； PDBConstruct 1–343； UniProt 19–361 Author chain Bt； PDBConstruct 1–343； UniProt 19–361 Author chain Bu； PDBConstruct 1–343； UniProt 19–361 Author chain Bv； PDBConstruct 1–343； UniProt 19–361 Author chain Bw； PDBConstruct 1–343； UniProt 19–361 Author chain Bx； PDBConstruct 1–343； UniProt 19–361 Author chain By； PDBConstruct 1–343； UniProt 19–361 Author chain Bz； PDBConstruct 1–343； UniProt 19–361

Flagellar protein FlgT

OrganismNot specified

UniProt Q9KPZ9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 156	Flagellar L-ring protein × 26 （Q9KQ13） Flagellar P-ring protein × 26 （Q9KQ14） Sodium-type flagellar protein MotY × 26 （Q9KT95） Flagellar assembly lipoprotein FlgP × 52 （A0A2V4N6M7）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KPZ9_VIBCH
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain Ca； PDBConstruct 1–352； UniProt 26–377 Author chain Cb； PDBConstruct 1–352； UniProt 26–377 Author chain Cc； PDBConstruct 1–352； UniProt 26–377 Author chain Cd； PDBConstruct 1–352； UniProt 26–377 Author chain Ce； PDBConstruct 1–352； UniProt 26–377 Author chain Cf； PDBConstruct 1–352； UniProt 26–377 Author chain Cg； PDBConstruct 1–352； UniProt 26–377 Author chain Ch； PDBConstruct 1–352； UniProt 26–377 Author chain Ci； PDBConstruct 1–352； UniProt 26–377 Author chain Cj； PDBConstruct 1–352； UniProt 26–377 Author chain Ck； PDBConstruct 1–352； UniProt 26–377 Author chain Cl； PDBConstruct 1–352； UniProt 26–377 Author chain Cm； PDBConstruct 1–352； UniProt 26–377 Author chain Cn； PDBConstruct 1–352； UniProt 26–377 Author chain Co； PDBConstruct 1–352； UniProt 26–377 Author chain Cp； PDBConstruct 1–352； UniProt 26–377 Author chain Cq； PDBConstruct 1–352； UniProt 26–377 Author chain Cr； PDBConstruct 1–352； UniProt 26–377 Author chain Cs； PDBConstruct 1–352； UniProt 26–377 Author chain Ct； PDBConstruct 1–352； UniProt 26–377 Author chain Cu； PDBConstruct 1–352； UniProt 26–377 Author chain Cv； PDBConstruct 1–352； UniProt 26–377 Author chain Cw； PDBConstruct 1–352； UniProt 26–377 Author chain Cx； PDBConstruct 1–352； UniProt 26–377 Author chain Cy； PDBConstruct 1–352； UniProt 26–377 Author chain Cz； PDBConstruct 1–352； UniProt 26–377

Sodium-type flagellar protein MotY

OrganismNot specified

UniProt Q9KT95

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 156	Flagellar L-ring protein × 26 （Q9KQ13） Flagellar P-ring protein × 26 （Q9KQ14） Flagellar protein FlgT × 26 （Q9KPZ9） Flagellar assembly lipoprotein FlgP × 52 （A0A2V4N6M7）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9KT95_VIBCH
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain Da； PDBConstruct 1–272； UniProt 23–294 Author chain Db； PDBConstruct 1–272； UniProt 23–294 Author chain Dc； PDBConstruct 1–272； UniProt 23–294 Author chain Dd； PDBConstruct 1–272； UniProt 23–294 Author chain De； PDBConstruct 1–272； UniProt 23–294 Author chain Df； PDBConstruct 1–272； UniProt 23–294 Author chain Dg； PDBConstruct 1–272； UniProt 23–294 Author chain Dh； PDBConstruct 1–272； UniProt 23–294 Author chain Di； PDBConstruct 1–272； UniProt 23–294 Author chain Dj； PDBConstruct 1–272； UniProt 23–294 Author chain Dk； PDBConstruct 1–272； UniProt 23–294 Author chain Dl； PDBConstruct 1–272； UniProt 23–294 Author chain Dm； PDBConstruct 1–272； UniProt 23–294 Author chain Dn； PDBConstruct 1–272； UniProt 23–294 Author chain Do； PDBConstruct 1–272； UniProt 23–294 Author chain Dp； PDBConstruct 1–272； UniProt 23–294 Author chain Dq； PDBConstruct 1–272； UniProt 23–294 Author chain Dr； PDBConstruct 1–272； UniProt 23–294 Author chain Ds； PDBConstruct 1–272； UniProt 23–294 Author chain Dt； PDBConstruct 1–272； UniProt 23–294 Author chain Du； PDBConstruct 1–272； UniProt 23–294 Author chain Dv； PDBConstruct 1–272； UniProt 23–294 Author chain Dw； PDBConstruct 1–272； UniProt 23–294 Author chain Dx； PDBConstruct 1–272； UniProt 23–294 Author chain Dy； PDBConstruct 1–272； UniProt 23–294 Author chain Dz； PDBConstruct 1–272； UniProt 23–294

Flagellar assembly lipoprotein FlgP

OrganismNot specified

UniProt A0A2V4N6M7

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 156	Flagellar L-ring protein × 26 （Q9KQ13） Flagellar P-ring protein × 26 （Q9KQ14） Flagellar protein FlgT × 26 （Q9KPZ9） Sodium-type flagellar protein MotY × 26 （Q9KT95）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0A2V4N6M7_VIBCL
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain Fa； PDBConstruct 1–15； UniProt 131–145 Author chain Fb； PDBConstruct 1–15； UniProt 131–145 Author chain Fc； PDBConstruct 1–15； UniProt 131–145 Author chain Fd； PDBConstruct 1–15； UniProt 131–145 Author chain Fe； PDBConstruct 1–15； UniProt 131–145 Author chain Ff； PDBConstruct 1–15； UniProt 131–145 Author chain Fg； PDBConstruct 1–15； UniProt 131–145 Author chain Fh； PDBConstruct 1–15； UniProt 131–145 Author chain Fi； PDBConstruct 1–15； UniProt 131–145 Author chain Fj； PDBConstruct 1–15； UniProt 131–145 Author chain Fk； PDBConstruct 1–15； UniProt 131–145 Author chain Fl； PDBConstruct 1–15； UniProt 131–145 Author chain Fm； PDBConstruct 1–15； UniProt 131–145 Author chain Fn； PDBConstruct 1–15； UniProt 131–145 Author chain Fo； PDBConstruct 1–15； UniProt 131–145 Author chain Fp； PDBConstruct 1–15； UniProt 131–145 Author chain Fq； PDBConstruct 1–15； UniProt 131–145 Author chain Fr； PDBConstruct 1–15； UniProt 131–145 Author chain Fs； PDBConstruct 1–15； UniProt 131–145 Author chain Ft； PDBConstruct 1–15； UniProt 131–145 Author chain Fu； PDBConstruct 1–15； UniProt 131–145 Author chain Fv； PDBConstruct 1–15； UniProt 131–145 Author chain Fw； PDBConstruct 1–15； UniProt 131–145 Author chain Fx； PDBConstruct 1–15； UniProt 131–145 Author chain Fy； PDBConstruct 1–15； UniProt 131–145 Author chain Fz； PDBConstruct 1–15； UniProt 131–145 Author chain Ga； PDBConstruct 1–15； UniProt 131–145 Author chain Gb； PDBConstruct 1–15； UniProt 131–145 Author chain Gc； PDBConstruct 1–15； UniProt 131–145 Author chain Gd； PDBConstruct 1–15； UniProt 131–145 Author chain Ge； PDBConstruct 1–15； UniProt 131–145 Author chain Gf； PDBConstruct 1–15； UniProt 131–145 Author chain Gg； PDBConstruct 1–15； UniProt 131–145 Author chain Gh； PDBConstruct 1–15； UniProt 131–145 Author chain Gi； PDBConstruct 1–15； UniProt 131–145 Author chain Gj； PDBConstruct 1–15； UniProt 131–145 Author chain Gk； PDBConstruct 1–15； UniProt 131–145 Author chain Gl； PDBConstruct 1–15； UniProt 131–145 Author chain Gm； PDBConstruct 1–15； UniProt 131–145 Author chain Gn； PDBConstruct 1–15； UniProt 131–145 Author chain Go； PDBConstruct 1–15； UniProt 131–145 Author chain Gp； PDBConstruct 1–15； UniProt 131–145 Author chain Gq； PDBConstruct 1–15； UniProt 131–145 Author chain Gr； PDBConstruct 1–15； UniProt 131–145 Author chain Gs； PDBConstruct 1–15； UniProt 131–145 Author chain Gt； PDBConstruct 1–15； UniProt 131–145 Author chain Gu； PDBConstruct 1–15； UniProt 131–145 Author chain Gv； PDBConstruct 1–15； UniProt 131–145 Author chain Gw； PDBConstruct 1–15； UniProt 131–145 Author chain Gx； PDBConstruct 1–15； UniProt 131–145 Author chain Gy； PDBConstruct 1–15； UniProt 131–145 Author chain Gz； PDBConstruct 1–15； UniProt 131–145

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	9ydo
Deposition date deposition_date	2025-09-22
Structure title title	LPHT-ring in Vibrio cholerae at assembled, opened state
Keywords keywords	In situ cryo-EM, sheathed flagellar motor, Vibrio cholerae, LP-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.

9ydo__assembly_1__model_1

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

Download this curve (.dat)

9ydo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9ydo__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)	120.70 Å
Total Rg	120.60 Å
Atom count	236015
Residues	30589
Excluded volume	4185200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9ydo__assembly_1__model_1`	156-meric （156）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Flagellar L-ring protein
Molecular weight formula_weight	24256.5 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Aa,Ab,Ac,Ad,Ae,Af,Ag,Ah,Ai,Aj,Ak,Al,Am,An,Ao,Ap,Aq,Ar,As,At,Au,Av,Aw,Ax,Ay,Az
Atom count atom_count	236015

TTTVDAVEGDKSESNSGLTDALRNRTDPVAGDPAWAPIHPKGKPEHYAAETGSLFNLASSSSMYDDSKPRGVGDIITVTLNESTKAAKSADADLNKKNDASMDPLAVGGKDLTIGDYNFSYALKNDNKFSGSAAANQSNSMSGSITVEVIEVLANGNLVIRGEKWLTLNTGDEYIRLSGTIRPDDIDFDNTIASNRISNARIQYSGTGTNQDMQEPGFLARFFNVSL

Entity 2 Entity 2 polymer

Description description	Flagellar P-ring protein
Molecular weight formula_weight	35702.6 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Ba,Bb,Bc,Bd,Be,Bf,Bg,Bh,Bi,Bj,Bk,Bl,Bm,Bn,Bo,Bp,Bq,Br,Bs,Bt,Bu,Bv,Bw,Bx,By,Bz

ARIKDVAQVAGVRNNQLVGYGLVTGLPGTGESTPFTDQSFNAMLQSFGIQLPPGTKPKTKNVAAVIVTADLPAFSKQGQTIDITVSSIGSAKSLRGGTLMQTFLKGLDGQVYAVAQGNLVVSGFSATGADGSKIVGNNPTVGMISSGAIVEREVPNPFGRGDYITFNLFESDFTTAQRLADAVNQFLGPQMASAVDAASIKVRAPRDLSQRVAFLSAIENLEFNPADSAAKIIVNSRTGTIVVGQNVRLKPAAVTHGGMTVAIKENLNVSQPNALGGGQTVVVPNTEIEVTEKQGKMFKLEPGVTLDDLVRAVNEVGAAPSDLMAILQALKQAGAIEGQLIII

Entity 3 Entity 3 polymer

Description description	Flagellar protein FlgT
Molecular weight formula_weight	39808.2 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Ca,Cb,Cc,Cd,Ce,Cf,Cg,Ch,Ci,Cj,Ck,Cl,Cm,Cn,Co,Cp,Cq,Cr,Cs,Ct,Cu,Cv,Cw,Cx,Cy,Cz

YEVTGSAAIVSSEEVARLHALEDALYKAVNFAGADIGSISNLMPLLESDRREYLFANHEVRYILIEERKAINNVMYVRTRIDIYPSATACHVEQYKKTMLIGNIDLASPQQAVMGQIYQVGDDFAQVINRRLEQESRSFVSVGTTQYDIDPKAPERIKMIAQDAGAQYIMGGMITDLTATIEQKTLQDDIINRQFAMEISVFDGKTGNEVMTRTYREVARWPFPKTSQIDTRSARFWASTYGEMMLRVSRNIMLDLESEISCKITLPQIVAKFGTTATMDLGRIHGVKQGDKLSLWHTGAFIDQQGLPRNKVTQSEITLTVSRVYEHEAELTVDQPELAYSIQIGDVMHKQM

Entity 4 Entity 4 polymer

Description description	Sodium-type flagellar protein MotY
Molecular weight formula_weight	31307.1 kDa
Source method src_method	nat
Copy count entity_count	26

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	Da,Db,Dc,Dd,De,Df,Dg,Dh,Di,Dj,Dk,Dl,Dm,Dn,Do,Dp,Dq,Dr,Ds,Dt,Du,Dv,Dw,Dx,Dy,Dz

LEVRYMATPQQSTWQMATNTPLECRLVHPIPNYGDAEFSSRAGKKINLDFELKMRRPMGDTRNVSLVSMPPVWRPGEGADRITNLQFFKQFDGYIGGQTAWSLLSELEKGRYPTFSYQDWQSRDQRIEVALSSVLFQQPYNEFSDCISKLLPYSFEDISFTILHYDQGTSVELNKASQKRLAQIAEYVRYNQDIDLVLVSTYTDSTDTNNNSQNLSEQRAEVLREYFKSIGLPEDRIQVQGYGKRRPIADNASPIGKDKNRRVVISLGRTQV

Entity 5 Entity 5 polymer

Description description	Flagellar assembly lipoprotein FlgP
Molecular weight formula_weight	1792.1 kDa
Source method src_method	nat
Copy count entity_count	52

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;Fa,Fb,Fc,Fd,Fe,Ff,Fg,Fh,Fi,Fj,Fk,Fl,Fm,Fn,Fo,Fp,Fq,Fr,Fs,Ft,Fu,Fv,Fw,Fx,Fy,Fz,Ga,Gb,Gc,Gd,Ge,Gf,Gg,Gh,Gi,Gj,Gk,Gl,Gm,Gn,Go,Gp,Gq,Gr,Gs,Gt,Gu,Gv,Gw,Gx,Gy,Gz ;

GEVQQVPEKRQMTLF

▶

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	2.69 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	112879

LPHT-ring in Vibrio cholerae at assembled, opened state

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

Flagellar protein FlgT

State in the Current Structure

Other States of the Same Protein in the Database

Sodium-type flagellar protein MotY

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar assembly lipoprotein FlgP

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

9ydo__assembly_1__model_1

9ydo__assembly_1__model_1 | I(q)

9ydo__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

7. Citations (1)

LPHT-ring in Vibrio cholerae at assembled, opened state

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

Flagellar protein FlgT

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Sodium-type flagellar protein MotY

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 assembly lipoprotein FlgP

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

9ydo__assembly_1__model_1

9ydo__assembly_1__model_1 | I(q)

9ydo__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

7. Citations (1)