SAXSdb — 1eg7

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

FORMYLTETRAHYDROFOLATE SYNTHETASE

Moorella thermoacetica

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	SULFATE ION × 22 water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	SULFATE ION × 11 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FTHS_MOOTH
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–557； UniProt 1–559 Author chain B； PDBConstruct 1–557； UniProt 1–559

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	1eg7
Deposition date deposition_date	2000-02-14
Structure title title	THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA
Keywords keywords	Synthetase, Folate Binding, ATP Binding, Formate Binding, Monovalent Cation Binding, 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.

1eg7__assembly_1__model_1

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

Download this curve (.dat)

1eg7__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1eg7__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	42.27 Å
Rg (electron density)	42.01 Å
Total Rg	42.27 Å
Atom count	16634
Residues	2194
Excluded volume	297730 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1eg7__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1eg7__assembly_2__model_1`	dimeric （2）	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 (3)

Entity 1 Entity 1 polymer

Description description	FORMYLTETRAHYDROFOLATE SYNTHETASE
Molecular weight formula_weight	59865.9 kDa
EC 编号 ec_number	6.3.4.3
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	8586

MSKVPSDIEIAQAAKMKPVMELARGLGIQEDEVELYGKYKAKISLDVYRRLKDKPDGKLILVTAITPTPAGEGKTTTSVGLTDALARLGKRVMVCLREPSLGPSFGIKGGAAGGGYAQVVPMEDINLHFTGDIHAVTYAHNLLAAMVDNHLQQGNVLNIDPRTITWRRVIDLNERALRNIVIGLGGKANGVPRETGFDISVASEVMACLCLASDLMDLKERFSRKVVGYTYDGKPVTAGDLEAQGSMALLMKDAIKPNLVQTLENTPAFIHGGPFANIAHGCNSIIATKTALKLADYVVTEAGFGADLGAEKFYDVKCRYAGFKPDATVIVATVRALKMHGGVPKSDLATENLEALREGFANLEKHIENIGKFGVPAVVAINAFPTDTEAELNLLYELCAKAGAEVALSWAKGGEGGLELARKVLQTLESRPSNFHVLYNLDLSIKDKIAKIATEIYGADGVNYTAEADKAIQRYESLGYGNLPVVMAKTQYSFSDDMTKLGRPRNFTITVREVRLSAGGRLIVPITGAIMTMPGLPKRPAACNIDIDADGVITGLF

Source Source

Source organism organism	Moorella thermoacetica
NCBI taxonomy ID ncbi_taxonomy_id	1525
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	11

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	269

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1eg7a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

Domain ID domain_id	d1eg7b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamily	c.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family family	c.37.1.10 — Nitrogenase iron protein-like

CATH v4.4 (6 domains)

Domain ID domain_id	1eg7A01
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	1eg7A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1510 — Domain 2, N(10)-formyltetrahydrofolate synthetase
Homologous superfamily homologous superfamily	10 — Domain 2, N(10)-formyltetrahydrofolate synthetase

Domain ID domain_id	1eg7A03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	410 — Formyltetrahydrofolate synthetase; domain 3
Homologous superfamily homologous superfamily	10 — Formyltetrahydrofolate synthetase, domain 3

Domain ID domain_id	1eg7B01
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	1eg7B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1510 — Domain 2, N(10)-formyltetrahydrofolate synthetase
Homologous superfamily homologous superfamily	10 — Domain 2, N(10)-formyltetrahydrofolate synthetase

Domain ID domain_id	1eg7B03
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	410 — Formyltetrahydrofolate synthetase; domain 3
Homologous superfamily homologous superfamily	10 — Formyltetrahydrofolate synthetase, domain 3

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Unit-cell length a length_a	160.876 Å
Unit-cell length b length_b	160.876 Å
Unit-cell length c length_c	256.118 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	36

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	19.990 Å
R factor r_factor	0.2530
R_work r_work	0.2530
R_free r_free	0.3010

THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA

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

FORMYLTETRAHYDROFOLATE SYNTHETASE

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

1eg7__assembly_1__model_1

1eg7__assembly_1__model_1 | I(q)

1eg7__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (1)

THE CRYSTAL STRUCTURE OF FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA

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

FORMYLTETRAHYDROFOLATE SYNTHETASE

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

1eg7__assembly_1__model_1

1eg7__assembly_1__model_1 | I(q)

1eg7__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

CATH v4.4 (6 domains)

7. Citations (1)