SAXSdb — 1oht

▼

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

CG14704 PROTEIN

DROSOPHILA MELANOGASTER

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	ZINC ION × 1 1,2-ETHANEDIOL × 2 L(+)-TARTARIC ACID × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9VGN3
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–215； UniProt 1–215

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	1oht
Deposition date deposition_date	2003-05-31
Structure title title	Peptidoglycan recognition protein LB
Keywords keywords	PEPTIDOGLYCAN-RECOGNITION PROTEIN-LB ISOFORM 2, HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1oht__assembly_1__model_1

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

Download this curve (.dat)

1oht__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1oht__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	16.27 Å
Rg (electron density)	15.09 Å
Total Rg	16.17 Å
Atom count	1387
Residues	168
Excluded volume	24613 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1oht__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	CG14704 PROTEIN
Molecular weight formula_weight	23961.1 kDa
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	1444

MQQANLGDGVATARLLSRSDWGARLPKSVEHFQGPAPYVIIHHSYMPAVCYSTPDCMKSMRDMQDFHQLERGWNDIGYSFGIGGDGMIYTGRGFNVIGAHAPKYNDKSVGIVLIGDWRTELPPKQMLDAAKNLIAFGVFKGYIDPAYKLLGHRQVRDTECPGGRLFAEISSWPHFTHINDTEGVSSTTAPVVPHVHPQAAAPQKPHQSPPAAPKV

Source Source

Source organism organism	DROSOPHILA MELANOGASTER
NCBI taxonomy ID ncbi_taxonomy_id	7227
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	L(+)-TARTARIC ACID
Molecular weight formula_weight	150.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	57

▼

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1ohta_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.118 — N-acetylmuramoyl-L-alanine amidase-like
Superfamily Superfamily superfamily	d.118.1 — N-acetylmuramoyl-L-alanine amidase-like
Family Family family	d.118.1.1 — N-acetylmuramoyl-L-alanine amidase-like

CATH v4.4 (1 domains)

Domain ID domain_id	1ohtA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	80 — Lysozyme-like
Homologous superfamily homologous superfamily	10 — Peptidoglycan recognition protein-like

▶

Unit-cell length a length_a	40.561 Å
Unit-cell length b length_b	40.561 Å
Unit-cell length c length_c	337.997 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	12

Space group space_group	P 61 2 2
Space-group number int_tables_number	178
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2160
R_work r_work	0.2160
R_free r_free	0.2430

Peptidoglycan recognition protein LB

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

CG14704 PROTEIN

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

1oht__assembly_1__model_1

1oht__assembly_1__model_1 | I(q)

1oht__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Peptidoglycan recognition protein LB

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

CG14704 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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1oht__assembly_1__model_1

1oht__assembly_1__model_1 | I(q)

1oht__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)