SAXSdb — 2hoe

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

N-acetylglucosamine kinase

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	POTASSIUM ION × 2 GLYCEROL × 2 water × 2	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	POTASSIUM ION × 1 GLYCEROL × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9X0V1_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–380； UniProt 1–368

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	2hoe
Deposition date deposition_date	2006-07-14
Structure title title	Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46 A resolution
Keywords keywords	;TM1224, N-acetylglucosamine kinase (EC 2.7.1.59), Structural Genomics, PSI-2, Protein Structure Initiative, Joint Center for Structural Genomics, JCSG, TRANSFERASE ;; TRANSFERASE
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.

2hoe__assembly_1__model_1

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

Download this curve (.dat)

2hoe__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2hoe__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.35 Å
Rg (electron density)	28.23 Å
Total Rg	29.10 Å
Atom count	5318
Residues	692
Excluded volume	95602 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2hoe__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2hoe__assembly_2__model_1`	monomeric （1）	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	N-acetylglucosamine kinase
Molecular weight formula_weight	42869.6 kDa
EC 编号 ec_number	2.7.1.59
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2674

MGSDKIHHHHHHMPKSVRAENISRILKRIMKSPVSRVELAEELGLTKTTVGEIAKIFLEKGIVVEEKDSPKGVGRPTKSLKISPNCAYVLGIEVTRDEIAACLIDASMNILAHEAHPLPSQSDREETLNVMYRIIDRAKDMMEKLGSKLSALTVAAPGPIDTERGIIIDPRNFPLSQIPLANLLKEKYGIEVWVENDADMGAVGEKWYTKRDDSFAWILTGKGIGAGIIIDGELYRGENGYAGEIGYTRVFNGNEYVFLEDVCNENVVLKHVLSMGFSSLAEARDSGDVRVKEYFDDIARYFSIGLLNLIHLFGISKIVIGGFFKELGENFLKKIKIEVETHLLYKHSVDMSFSKVQEPVIAFGAAVHALENYLERVTTS

Source Source

Source organism organism	Thermotoga maritima
NCBI taxonomy ID ncbi_taxonomy_id	2336
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	15

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2hoea1
Class class	a — All alpha proteins
Fold Fold fold	a.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamily	a.4.5 — 'Winged helix' DNA-binding domain
Family Family family	a.4.5.63 — ROK associated domain

Domain ID domain_id	d2hoea2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamily	c.55.1 — Actin-like ATPase domain
Family Family family	c.55.1.10 — ROK

Domain ID domain_id	d2hoea3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamily	c.55.1 — Actin-like ATPase domain
Family Family family	c.55.1.10 — ROK

CATH v4.4 (3 domains)

Domain ID domain_id	2hoeA01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily	10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Domain ID domain_id	2hoeA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

Domain ID domain_id	2hoeA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily	40 — ATPase, nucleotide binding domain

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Unit-cell length a length_a	62.599 Å
Unit-cell length b length_b	62.599 Å
Unit-cell length c length_c	173.950 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	6

Space group space_group	P 31 1 2
Space-group number int_tables_number	151
Crystal system crystal_system	—

Resolution resolution	2.460 Å
Low-resolution limit resolution_low	33.930 Å
R factor r_factor	0.2190
R_work r_work	0.2160
R_free r_free	0.2710

Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46 A resolution

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

N-acetylglucosamine kinase

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

2hoe__assembly_1__model_1

2hoe__assembly_1__model_1 | I(q)

2hoe__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)

Crystal structure of N-acetylglucosamine kinase (TM1224) from Thermotoga maritima at 2.46 A resolution

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

N-acetylglucosamine kinase

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

2hoe__assembly_1__model_1

2hoe__assembly_1__model_1 | I(q)

2hoe__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (1)