1kkm

L.casei HprK/P in complex with B.subtilis P-Ser-HPr

Method: X-RAY DIFFRACTION

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

HprK protein

Lactobacillus casei

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	PHOSPHOCARRIER PROTEIN HPR × 6 （P08877） CALCIUM ION × 6 PHOSPHATE ION × 6 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HPRK_LACCA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 14–205； UniProt 128–319 Author chain B； PDBConstruct 14–205； UniProt 128–319 Author chain C； PDBConstruct 14–205； UniProt 128–319

PHOSPHOCARRIER PROTEIN HPR

Bacillus subtilis

UniProt P08877

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 12	HprK protein × 6 （Q9RE09） CALCIUM ION × 6 PHOSPHATE ION × 6 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PTHP_BACSU
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 13–100； UniProt 0–87 Author chain I； PDBConstruct 13–100； UniProt 0–87 Author chain J； PDBConstruct 13–100； UniProt 0–87

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	1kkm
Deposition date deposition_date	2001-12-10
Structure title title	L.casei HprK/P in complex with B.subtilis P-Ser-HPr
Keywords keywords	;phosphorylation, protein kinase, bacteria, protein/protein interaction, phosphoserine, TRANSFERASE, HYDROLASE-TRANSPORT PROTEIN COMPLEX ;; TRANSFERASE,HYDROLASE/TRANSPORT PROTEIN
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.

1kkm__assembly_1__model_1

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

Download this curve (.dat)

1kkm__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1kkm__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.10 Å
Rg (electron density)	34.88 Å
Total Rg	35.24 Å
Atom count	11760
Residues	1572
Excluded volume	209080 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1kkm__assembly_1__model_1`	dodecameric （12）	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 (5)

Entity 1 Entity 1 polymer

Description description	HprK protein
Molecular weight formula_weight	22679.7 kDa
EC 编号 ec_number	2.7.1.-, 3.1.3.-
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	6051

MRGSHHHHHHGSMYLDSQLAERRSMHGVLVDIYGLGVLITGDSGVGKSETALELVQRGHRLIADDRVDVYQQDEQTIVGAAPPILSHLLEIRGLGIIDVMNLFGAGAVREDTTISLIVHLENWTPDKTFDRLGSGEQTQLIFDVPVPKITVPVKVGRNLAIIIEVAAMNFRAKSMGYDATKTFEKNLNHLIEHNEETDQNSSGDK

Source Source

Source organism organism	Lactobacillus casei
NCBI taxonomy ID ncbi_taxonomy_id	1582
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	PHOSPHOCARRIER PROTEIN HPR
Molecular weight formula_weight	10784.0 kDa
Mutation mutation	G85R
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J

MRGSHHHHHHGSMAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAEITISASGADENDALNALEETMKSERLGE

Source Source

Source organism organism	Bacillus subtilis
NCBI taxonomy ID ncbi_taxonomy_id	1423
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	171

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1kkma_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.91 — PEP carboxykinase-like
Superfamily Superfamily superfamily	c.91.1 — PEP carboxykinase-like
Family Family family	c.91.1.2 — HPr kinase HprK C-terminal domain

Domain ID domain_id	d1kkmb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.91 — PEP carboxykinase-like
Superfamily Superfamily superfamily	c.91.1 — PEP carboxykinase-like
Family Family family	c.91.1.2 — HPr kinase HprK C-terminal domain

Domain ID domain_id	d1kkmc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.91 — PEP carboxykinase-like
Superfamily Superfamily superfamily	c.91.1 — PEP carboxykinase-like
Family Family family	c.91.1.2 — HPr kinase HprK C-terminal domain

Domain ID domain_id	d1kkmh_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

Domain ID domain_id	d1kkmi_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

Domain ID domain_id	d1kkmj_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.94 — HPr-like
Superfamily Superfamily superfamily	d.94.1 — HPr-like
Family Family family	d.94.1.1 — HPr-like

CATH v4.4 (6 domains)

Domain ID domain_id	1kkmA00
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	1kkmB00
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	1kkmC00
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	1kkmH00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

Domain ID domain_id	1kkmI00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

Domain ID domain_id	1kkmJ00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1340 — Histidine-containing Protein; Chain: A;
Homologous superfamily homologous superfamily	10 — HPr-like

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Unit-cell length a length_a	80.832 Å
Unit-cell length b length_b	80.832 Å
Unit-cell length c length_c	252.488 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	P 32 1 2
Space-group number int_tables_number	153
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	—
R_work r_work	0.2000
R_free r_free	0.2570

L.casei HprK/P in complex with B.subtilis P-Ser-HPr

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

HprK protein

State in the Current Structure

Other States of the Same Protein in the Database

PHOSPHOCARRIER PROTEIN HPR

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

1kkm__assembly_1__model_1

1kkm__assembly_1__model_1 | I(q)

1kkm__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

L.casei HprK/P in complex with B.subtilis P-Ser-HPr

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

HprK 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

PHOSPHOCARRIER PROTEIN HPR

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

1kkm__assembly_1__model_1

1kkm__assembly_1__model_1 | I(q)

1kkm__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 (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)