SAXSdb — 1o5z

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

folylpolyglutamate synthase/dihydrofolate synthase

Thermotoga maritima

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 4 CHLORIDE ION × 2 UNKNOWN LIGAND × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9WY13_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 13–442； UniProt 1–430

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	1o5z
Deposition date deposition_date	2003-10-10
Structure title title	Crystal structure of Folylpolyglutamate synthase (TM0166) from Thermotoga maritima at 2.10 A resolution
Keywords keywords	;TM0166, FOLYLPOLYGLUTAMATE SYNTHASE, STRUCTURAL GENOMICS, JCSG, PSI, Protein Structure Initiative, Joint Center for Structural Genomics, LIGASE ;; LIGASE
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.

1o5z__assembly_1__model_1

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

Download this curve (.dat)

1o5z__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1o5z__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.88 Å
Rg (electron density)	21.86 Å
Total Rg	22.74 Å
Atom count	3393
Residues	421
Excluded volume	60779 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1o5z__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	folylpolyglutamate synthase/dihydrofolate synthase
Molecular weight formula_weight	50399.0 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	3716

MGSDKIHHHHHHMAYLEVLRYLYHKRPMGKVKPGLERISMLLSKLGNPHLEYKTIHIGGTNGKGSVANMVSNILVSQGYRVGSYYSPHLSTFRERIRLNEEYISEEDVVKIYETMEPILNELDKEEIFSPSFFEVVTAMAFLYFAEKNVDIAVLEVGLGGRLDATNVVFPLCSTIVTVDRDHEKTLGYTIEQIAWEKSGIIKERVPLVTGERKREALKVMEDVARKKSSRMYVIDKDFSVKVKSLKLHENRFDYCGENTFEDLVLTMNGPHQIENAGVALKTLEATGLPLSEKAIREGLKNAKNLGRFEILEKNGKMYILDGAHNPHGAESLVRSLKLYFNGEPLSLVIGILDDKNREDILRKYTGIFERVIVTRVPSPRMKDMNSLVDMAKKFFKNVEVIEDPLEAIESTERATVVTGSLFLVGYVREFLTTGKINEEWKL

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	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	UNKNOWN LIGAND
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	323

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1o5za1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.59 — MurD-like peptide ligases, peptide-binding domain
Superfamily Superfamily superfamily	c.59.1 — MurD-like peptide ligases, peptide-binding domain
Family Family family	c.59.1.2 — Folylpolyglutamate synthetase, C-terminal domain

Domain ID domain_id	d1o5za2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.72 — Ribokinase-like
Superfamily Superfamily superfamily	c.72.2 — MurD-like peptide ligases, catalytic domain
Family Family family	c.72.2.2 — Folylpolyglutamate synthetase

Domain ID domain_id	d1o5za3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	1o5zA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1190 — UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
Homologous superfamily homologous superfamily	10 — Mur-like, catalytic domain

Domain ID domain_id	1o5zA02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily	20 — Mur ligase, C-terminal domain

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Unit-cell length a length_a	84.751 Å
Unit-cell length b length_b	84.751 Å
Unit-cell length c length_c	280.679 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	2.100 Å
Low-resolution limit resolution_low	35.190 Å
R factor r_factor	0.1842
R_work r_work	0.1811
R_free r_free	0.2442

Crystal structure of Folylpolyglutamate synthase (TM0166) from Thermotoga maritima at 2.10 A resolution

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

folylpolyglutamate synthase/dihydrofolate synthase

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

1o5z__assembly_1__model_1

1o5z__assembly_1__model_1 | I(q)

1o5z__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) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of Folylpolyglutamate synthase (TM0166) from Thermotoga maritima at 2.10 A resolution

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

folylpolyglutamate synthase/dihydrofolate synthase

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

1o5z__assembly_1__model_1

1o5z__assembly_1__model_1 | I(q)

1o5z__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) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

7. Citations (1)