SAXSdb — 9paw

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

Protein HflK

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 24	Modulator of FtsH protease HflC × 12 （P0ABC5）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HFLK_ECO57
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain XA； PDBConstruct 1–419； UniProt 1–419 Author chain XC； PDBConstruct 1–419； UniProt 1–419 Author chain XE； PDBConstruct 1–419； UniProt 1–419 Author chain XG； PDBConstruct 1–419； UniProt 1–419 Author chain XI； PDBConstruct 1–419； UniProt 1–419 Author chain XK； PDBConstruct 1–419； UniProt 1–419 Author chain XM； PDBConstruct 1–419； UniProt 1–419 Author chain XO； PDBConstruct 1–419； UniProt 1–419 Author chain XQ； PDBConstruct 1–419； UniProt 1–419 Author chain XS； PDBConstruct 1–419； UniProt 1–419 Author chain XU； PDBConstruct 1–419； UniProt 1–419 Author chain XW； PDBConstruct 1–419； UniProt 1–419

Modulator of FtsH protease HflC

Escherichia coli

UniProt P0ABC5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 24	Protein HflK × 12 （P0ABC8）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HFLC_ECO57
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain XB； PDBConstruct 1–334； UniProt 1–334 Author chain XD； PDBConstruct 1–334； UniProt 1–334 Author chain XF； PDBConstruct 1–334； UniProt 1–334 Author chain XH； PDBConstruct 1–334； UniProt 1–334 Author chain XJ； PDBConstruct 1–334； UniProt 1–334 Author chain XL； PDBConstruct 1–334； UniProt 1–334 Author chain XN； PDBConstruct 1–334； UniProt 1–334 Author chain XP； PDBConstruct 1–334； UniProt 1–334 Author chain XR； PDBConstruct 1–334； UniProt 1–334 Author chain XT； PDBConstruct 1–334； UniProt 1–334 Author chain XV； PDBConstruct 1–334； UniProt 1–334 Author chain XX； PDBConstruct 1–334； UniProt 1–334

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	9paw
Deposition date deposition_date	2025-06-25
Structure title title	Cryo-EM structure of the engineered HflK/C variant stabilized in the closed conformation via disulfide bond crosslinking.
Keywords keywords	FtsH, HflK, HflC, CHAPERONE, AAA protease; CHAPERONE
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.

9paw__assembly_1__model_1

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

Download this curve (.dat)

9paw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9paw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	82.88 Å
Rg (electron density)	83.31 Å
Total Rg	83.11 Å
Atom count	103604
Residues	6468
Excluded volume	918820 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9paw__assembly_1__model_1`	24-meric （24）	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 (2)

Entity 1 Entity 1 polymer

Description description	Protein HflK
Molecular weight formula_weight	45662.9 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	XA,XC,XE,XG,XI,XK,XM,XO,XQ,XS,XU,XW
Atom count atom_count	103604

MAWNQPGNNGQDRDPWGSSKPGGNSEGNGNKGGRDQGPPDLDDIFRKLSKKLGGLGGGKGTGSGGGSSSQGPRPQLGGRVVTIAAAAIVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTNPEKYLYSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGITLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAECYTNEVQPRANGQCQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPEITRERLYIETMEKVLGNTRKVLVNDKGGNLMVLPLDQMLKGGNAPAAKSDNGASNLLRLPPASSSTTSGASNTSSTSQGDIMDQRRANAQRNDYQRQGE

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Modulator of FtsH protease HflC
Molecular weight formula_weight	37768.0 kDa
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	XB,XD,XF,XH,XJ,XL,XN,XP,XR,XT,XV,XX

MRKSVIAIIIIVLVVLYMSVFVVKEGERGITLRFGKVLRDDDNKPLVYEPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKEKKDLIVDSYIKWRISDFSRYYLATGGGDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTDSRGRLTLEVRDALNSGSAGTEDEVTTPAADNAIAEAAERVTAETKGKVPVINPNSMAALGIEVVDVRIKQINLPTEVSEAIYNRMRAERECVARRHRSQGQEEAEKLRATADYEVTRTLAECERQGRIMRGEGDAEAAKLFADAFSKDPDFYAFIRSLRAYENSFSGNQDVMVMSPDSDFFRYMKTPTSATR

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli BL21(DE3)

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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	2.93 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	299919

Cryo-EM structure of the engineered HflK/C variant stabilized in the closed conformation via disulfide bond crosslinking.

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

Protein HflK

State in the Current Structure

Other States of the Same Protein in the Database

Modulator of FtsH protease HflC

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

9paw__assembly_1__model_1

9paw__assembly_1__model_1 | I(q)

9paw__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)

Cryo-EM structure of the engineered HflK/C variant stabilized in the closed conformation via disulfide bond crosslinking.

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

Protein HflK

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Modulator of FtsH protease HflC

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

9paw__assembly_1__model_1

9paw__assembly_1__model_1 | I(q)

9paw__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

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

7. Citations (1)