SAXSdb — 2fmt

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

METHIONYL-TRNA FMET FORMYLTRANSFERASE

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein–RNA	Monomer	Protein 1 RNA 1	FORMYL-METHIONYL-TRNAFMET2 × 1 MAGNESIUM ION × 1 N-FORMYLMETHIONINE × 1 water × 2	Consistent with all polymers
2	Protein–RNA	Monomer	Protein 1 RNA 1	FORMYL-METHIONYL-TRNAFMET2 × 1 MAGNESIUM ION × 1 N-FORMYLMETHIONINE × 1 water × 2	Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FMT_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–314； UniProt 1–314 Author chain B； PDBConstruct 1–314； UniProt 1–314

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	2fmt
Deposition date deposition_date	1998-07-29
Structure title title	METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET
Keywords keywords	COMPLEX (METHYLTRANSFERASE-TRNA), FORMYLTRANSFERASE, INITIATION OF TRANSLATION, COMPLEX (METHYLTRANSFERASE-TRNA) complex; COMPLEX (METHYLTRANSFERASE/TRNA)
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.

2fmt__assembly_1__model_1

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

Download this curve (.dat)

2fmt__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2fmt__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.59 Å
Rg (electron density)	29.18 Å
Total Rg	29.76 Å
Atom count	4048
Residues	386
Excluded volume	66437 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2fmt__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2fmt__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 (5)

Entity 1 Entity 1 polymer

Description description	FORMYL-METHIONYL-TRNAFMET2
Molecular weight formula_weight	24832.9 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	C,D
Atom count atom_count	8179

CGCGGGGUGGAGCAGCCUGGUAGCUCGUCGGGCUCAUAACCCGAAGAUCGUCGGUUCAAAUCCGGCCCCCGCAACCA

Entity 2 Entity 2 polymer

Description description	METHIONYL-TRNA FMET FORMYLTRANSFERASE
Molecular weight formula_weight	34071.2 kDa
EC 编号 ec_number	2.1.2.9
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B

SESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSPVKVLAEEKGLPVFQPVSLRPQENQQLVAELQADVMVVVAYGLILPKAVLEMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDMLYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETLVTYAEKLSKEEARIDWSLSAAQLERCIRAFNPWPMSWLEIEGQPVKVWKASVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLLNSRREWFVPGNRLV

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	N-FORMYLMETHIONINE
Molecular weight formula_weight	177.2 kDa
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	83

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d2fmta1
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	d2fmta2
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

Domain ID domain_id	d2fmtb1
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	d2fmtb2
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 (4 domains)

Domain ID domain_id	2fmtA01
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	2fmtA02
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

Domain ID domain_id	2fmtB01
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	2fmtB02
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	201.710 Å
Unit-cell length b length_b	68.060 Å
Unit-cell length c length_c	86.350 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	8

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

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	19.000 Å
R factor r_factor	0.2470
R_work r_work	0.2470
R_free r_free	0.2920

METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET

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

METHIONYL-TRNA FMET FORMYLTRANSFERASE

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

2fmt__assembly_1__model_1

2fmt__assembly_1__model_1 | I(q)

2fmt__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

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-TRNAFMET

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

METHIONYL-TRNA FMET FORMYLTRANSFERASE

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

2fmt__assembly_1__model_1

2fmt__assembly_1__model_1 | I(q)

2fmt__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

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)