SAXSdb — 3r9i

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

Septum site-determining protein minD

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Cell division topological specificity factor × 2 （P0A734） ADENOSINE-5'-DIPHOSPHATE × 2 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Cell division topological specificity factor × 2 （P0A734） ADENOSINE-5'-DIPHOSPHATE × 2 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MIND_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–260； UniProt 1–260 Author chain B； PDBConstruct 1–260； UniProt 1–260 Author chain C； PDBConstruct 1–260； UniProt 1–260 Author chain D； PDBConstruct 1–260； UniProt 1–260

Cell division topological specificity factor

OrganismNot specified

UniProt P0A734

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 4	Septum site-determining protein minD × 2 （P0AEZ3） ADENOSINE-5'-DIPHOSPHATE × 2 water × 4	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	Septum site-determining protein minD × 2 （P0AEZ3） ADENOSINE-5'-DIPHOSPHATE × 2 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MINE_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–20； UniProt 12–31 Author chain F； PDBConstruct 1–20； UniProt 12–31 Author chain G； PDBConstruct 1–20； UniProt 12–31 Author chain H； PDBConstruct 1–20； UniProt 12–31

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	3r9i
Deposition date deposition_date	2011-03-25
Structure title title	2.6A resolution structure of MinD complexed with MinE (12-31) peptide
Keywords keywords	ATPase, bacterial cell division inhibitor, mine, CELL CYCLE, HYDROLASE-CELL CYCLE complex; CELL CYCLE,HYDROLASE/CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

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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.

3r9i__assembly_1__model_1

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

Download this curve (.dat)

3r9i__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3r9i__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	23.34 Å
Rg (electron density)	22.26 Å
Total Rg	23.07 Å
Atom count	4152
Residues	539
Excluded volume	74083 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3r9i__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3r9i__assembly_2__model_1`	tetrameric （4）	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 (4)

Entity 1 Entity 1 polymer

Description description	Septum site-determining protein minD
Molecular weight formula_weight	28500.7 kDa
Mutation mutation	D40A
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	8467

MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFAIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEK

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	83333
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Cell division topological specificity factor
Molecular weight formula_weight	2385.8 kDa
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

KNTANIAKERLQIIVAERRR

Entity 3 Entity 3 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	177

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3r9iA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3r9iB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3r9iC00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

Domain ID domain_id	3r9iD00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	300 — P-loop containing nucleotide triphosphate hydrolases

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Unit-cell length a length_a	64.293 Å
Unit-cell length b length_b	71.796 Å
Unit-cell length c length_c	76.644 Å
Unit-cell angle α angle_alpha	102.64 °
Unit-cell angle β angle_beta	95.87 °
Unit-cell angle γ angle_gamma	111.72 °
Molecules per unit cell Z z_pdb	4

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

Resolution resolution	2.600 Å
Low-resolution limit resolution_low	43.417 Å
R factor r_factor	0.2033
R_work r_work	0.2012
R_free r_free	0.2426

2.6A resolution structure of MinD complexed with MinE (12-31) peptide

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

Septum site-determining protein minD

State in the Current Structure

Other States of the Same Protein in the Database

Cell division topological specificity factor

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

3r9i__assembly_1__model_1

3r9i__assembly_1__model_1 | I(q)

3r9i__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

2.6A resolution structure of MinD complexed with MinE (12-31) peptide

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

Septum site-determining protein minD

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 topological specificity factor

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

3r9i__assembly_1__model_1

3r9i__assembly_1__model_1 | I(q)

3r9i__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)