SAXSdb — 1s3i

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

10-formyltetrahydrofolate dehydrogenase

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	BETA-MERCAPTOETHANOL × 5 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FTHFD_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–310； UniProt 1–310

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	1s3i
Deposition date deposition_date	2004-01-13
Structure title title	Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase
Keywords keywords	Rossmann fold, HYDROLASE, OXIDOREDUCTASE; HYDROLASE, OXIDOREDUCTASE
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.

1s3i__assembly_1__model_1

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

Download this curve (.dat)

1s3i__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1s3i__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.95 Å
Rg (electron density)	22.18 Å
Total Rg	23.06 Å
Atom count	2400
Residues	307
Excluded volume	42893 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1s3i__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 (3)

Entity 1 Entity 1 polymer

Description description	10-formyltetrahydrofolate dehydrogenase
Molecular weight formula_weight	34081.8 kDa
EC 编号 ec_number	1.5.1.6
Mutation mutation	none
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	2453

MKIAVIGQSLFGQEVYCQLRKEGHEVVGVFTIPDKDGKADPDGLEAEKDGVPVFKFPRWRARGQALPEVVAKYQALGAELNVLPFCSQFIPMEVINAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFTIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGTAPRCPQSEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACGQKLTFFNSTLNTSGLSTQGEALPIPGAHRPGVVTKAGLILFGNDDRMLLVKNIQLEDGKMMPASQFFKGSD

Source Source

Source organism organism	Rattus norvegicus
Common name common_name	Norway rat
NCBI taxonomy ID ncbi_taxonomy_id	10116
Host organism host_organism	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	BETA-MERCAPTOETHANOL
Molecular weight formula_weight	78.1 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	53

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1s3ia1
Class class	b — All beta proteins
Fold Fold fold	b.46 — FMT C-terminal domain-like
Superfamily Superfamily superfamily	b.46.1 — FMT C-terminal domain-like
Family Family family	b.46.1.1 — Post formyltransferase domain

Domain ID domain_id	d1s3ia2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.65 — Formyltransferase
Superfamily Superfamily superfamily	c.65.1 — Formyltransferase
Family Family family	c.65.1.1 — Formyltransferase

CATH v4.4 (2 domains)

Domain ID domain_id	1s3iA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	170 — Formyl transferase, N-terminal domain

Domain ID domain_id	1s3iA02
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	25 — Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — Formyl transferase, C-terminal domain

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Unit-cell length a length_a	100.000 Å
Unit-cell length b length_b	64.630 Å
Unit-cell length c length_c	64.590 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2453
R_work r_work	0.2420
R_free r_free	0.3053

Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

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

10-formyltetrahydrofolate dehydrogenase

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

1s3i__assembly_1__model_1

1s3i__assembly_1__model_1 | I(q)

1s3i__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

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

10-formyltetrahydrofolate dehydrogenase

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

1s3i__assembly_1__model_1

1s3i__assembly_1__model_1 | I(q)

1s3i__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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (2)