SAXSdb — 9iue

▼

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

Cell division protein ZipA

Escherichia coli str. K-12 substr. MG1655

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 54	Cell division ATP-binding protein FtsE × 18 （W1F1D8） Cell division protein FtsX × 18 （P0AC30） PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 18	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ZIPA_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–328； UniProt 1–328 Author chain 2； PDBConstruct 1–328； UniProt 1–328 Author chain E； PDBConstruct 1–328； UniProt 1–328 Author chain F； PDBConstruct 1–328； UniProt 1–328 Author chain K； PDBConstruct 1–328； UniProt 1–328 Author chain L； PDBConstruct 1–328； UniProt 1–328 Author chain Q； PDBConstruct 1–328； UniProt 1–328 Author chain R； PDBConstruct 1–328； UniProt 1–328 Author chain W； PDBConstruct 1–328； UniProt 1–328 Author chain X； PDBConstruct 1–328； UniProt 1–328 Author chain c； PDBConstruct 1–328； UniProt 1–328 Author chain d； PDBConstruct 1–328； UniProt 1–328 Author chain i； PDBConstruct 1–328； UniProt 1–328 Author chain j； PDBConstruct 1–328； UniProt 1–328 Author chain o； PDBConstruct 1–328； UniProt 1–328 Author chain p； PDBConstruct 1–328； UniProt 1–328 Author chain u； PDBConstruct 1–328； UniProt 1–328 Author chain v； PDBConstruct 1–328； UniProt 1–328

Cell division ATP-binding protein FtsE

Escherichia coli str. K-12 substr. MG1655

UniProt W1F1D8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 54	Cell division protein ZipA × 18 （P77173） Cell division protein FtsX × 18 （P0AC30） PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 18	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	W1F1D8_ECOLX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain 5； PDBConstruct 2–226； UniProt 194–418 Author chain 6； PDBConstruct 2–226； UniProt 194–418 Author chain G； PDBConstruct 2–226； UniProt 194–418 Author chain H； PDBConstruct 2–226； UniProt 194–418 Author chain M； PDBConstruct 2–226； UniProt 194–418 Author chain N； PDBConstruct 2–226； UniProt 194–418 Author chain S； PDBConstruct 2–226； UniProt 194–418 Author chain T； PDBConstruct 2–226； UniProt 194–418 Author chain Y； PDBConstruct 2–226； UniProt 194–418 Author chain Z； PDBConstruct 2–226； UniProt 194–418 Author chain e； PDBConstruct 2–226； UniProt 194–418 Author chain f； PDBConstruct 2–226； UniProt 194–418 Author chain k； PDBConstruct 2–226； UniProt 194–418 Author chain l； PDBConstruct 2–226； UniProt 194–418 Author chain q； PDBConstruct 2–226； UniProt 194–418 Author chain r； PDBConstruct 2–226； UniProt 194–418 Author chain w； PDBConstruct 2–226； UniProt 194–418 Author chain x； PDBConstruct 2–226； UniProt 194–418

Cell division protein FtsX

Escherichia coli str. K-12 substr. MG1655

UniProt P0AC30

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 54	Cell division protein ZipA × 18 （P77173） Cell division ATP-binding protein FtsE × 18 （W1F1D8） PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 18	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FTSX_ECOLI
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–352； UniProt 1–352 Author chain B； PDBConstruct 1–352； UniProt 1–352 Author chain C； PDBConstruct 1–352； UniProt 1–352 Author chain D； PDBConstruct 1–352； UniProt 1–352 Author chain I； PDBConstruct 1–352； UniProt 1–352 Author chain J； PDBConstruct 1–352； UniProt 1–352 Author chain O； PDBConstruct 1–352； UniProt 1–352 Author chain P； PDBConstruct 1–352； UniProt 1–352 Author chain U； PDBConstruct 1–352； UniProt 1–352 Author chain V； PDBConstruct 1–352； UniProt 1–352 Author chain a； PDBConstruct 1–352； UniProt 1–352 Author chain b； PDBConstruct 1–352； UniProt 1–352 Author chain g； PDBConstruct 1–352； UniProt 1–352 Author chain h； PDBConstruct 1–352； UniProt 1–352 Author chain m； PDBConstruct 1–352； UniProt 1–352 Author chain n； PDBConstruct 1–352； UniProt 1–352 Author chain s； PDBConstruct 1–352； UniProt 1–352 Author chain t； PDBConstruct 1–352； UniProt 1–352

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	9iue
Deposition date deposition_date	2024-07-20
Structure title title	cryo-EM structure of FtsE/X and ZipA complex in filament
Keywords keywords	cell division, division filament, FtsE/X, ZipA, CELL CYCLE; CELL CYCLE
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.

9iue__assembly_1__model_1

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

Download this curve (.dat)

9iue__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9iue__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	92.71 Å
Rg (electron density)	92.73 Å
Total Rg	92.31 Å
Atom count	75492
Residues	9846
Excluded volume	1356600 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9iue__assembly_1__model_1`	54-meric （54）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Cell division protein ZipA
Molecular weight formula_weight	36517.2 kDa
Source method src_method	man
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,E,F,K,L,Q,R,W,X,c,d,i,j,o,p,u,v
Atom count atom_count	75492

MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA

Source Source

Source organism organism	Escherichia coli str. K-12 substr. MG1655
NCBI taxonomy ID ncbi_taxonomy_id	511145
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Cell division ATP-binding protein FtsE
Molecular weight formula_weight	24832.7 kDa
Source method src_method	man
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	5,6,G,H,M,N,S,T,Y,Z,e,f,k,l,q,r,w,x

SGLVMIRFEHVSKAYLGGRQALQGVTFHMQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDINLISRRSYRMLTLSDGHLHGGVGHE

Source Source

Source organism organism	Escherichia coli str. K-12 substr. MG1655
NCBI taxonomy ID ncbi_taxonomy_id	511145
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 3 Entity 3 polymer

Description description	Cell division protein FtsX
Molecular weight formula_weight	38583.5 kDa
Source method src_method	man
Copy count entity_count	18

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,I,J,O,P,U,V,a,b,g,h,m,n,s,t

MNKRDAINHIRQFGGRLDRFRKSVGGSGDGGRNAPKRAKSSPKPVNRKTNVFNEQVRYAFHGALQDLKSKPFATFLTVMVIAISLTLPSVCYMVYKNVNQAATQYYPSPQITVYLQKTLDDDAAAGVVAQLQAEQGVEKVNYLSREDALGEFRNWSGFGGALDMLEENPLPAVAVVIPKLDFQGTESLNTLRDRITQINGIDEVRMDDSWFARLAALTGLVGRVSAMIGVLMVAAVFLVIGNSVRLSIFARRDSINVQKLIGATDGFILRPFLYGGALLGFSGALLSLILSEILVLRLSSAVAEVAQVFGTKFDINGLSFDECLLLLLVCSMIGWVAAWLATVQHLRHFTPE

Source Source

Source organism organism	Escherichia coli str. K-12 substr. MG1655
NCBI taxonomy ID ncbi_taxonomy_id	511145
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 4 Entity 4 non-polymer

Description description	PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
Molecular weight formula_weight	523.2 kDa
Source method src_method	syn
Copy count entity_count	18

▶

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	3.300 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

cryo-EM structure of FtsE/X and ZipA complex in filament

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

Cell division protein ZipA

State in the Current Structure

Other States of the Same Protein in the Database

Cell division ATP-binding protein FtsE

State in the Current Structure

Other States of the Same Protein in the Database

Cell division protein FtsX

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

9iue__assembly_1__model_1

9iue__assembly_1__model_1 | I(q)

9iue__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

7. Citations (1)

cryo-EM structure of FtsE/X and ZipA complex in filament

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

Cell division protein ZipA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cell division ATP-binding protein FtsE

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cell division protein FtsX

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

9iue__assembly_1__model_1

9iue__assembly_1__model_1 | I(q)

9iue__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 non-polymer

7. Citations (1)