2pfd

Anisotropically refined structure of FTCD

Method: X-RAY DIFFRACTION

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

Formimidoyltransferase-cyclodeaminase

Rattus norvegicus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 8	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 8	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FTCD_RAT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–541； UniProt 1–541 Author chain B； PDBConstruct 1–541； UniProt 1–541 Author chain C； PDBConstruct 1–541； UniProt 1–541 Author chain D； PDBConstruct 1–541； UniProt 1–541

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	2pfd
Deposition date deposition_date	2007-04-04
Structure title title	Anisotropically refined structure of FTCD
Keywords keywords	Protein assembly, Transferase, Lyase; Transferase, Lyase
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.

2pfd__assembly_1__model_1

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

Download this curve (.dat)

2pfd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2pfd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	59.41 Å
Rg (electron density)	58.60 Å
Total Rg	58.92 Å
Atom count	33048
Residues	4256
Excluded volume	590190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2pfd__assembly_1__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2pfd__assembly_2__model_1`	octameric （8）	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 (1)

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6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id	2pfdA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	990 — Formiminotransferase-cyclodeaminase; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Formiminotransferase, N-terminal subdomain

Domain ID domain_id	2pfdA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	670 — Formiminotransferase, C-terminal subdomain

Domain ID domain_id	2pfdA03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	680 — Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle

Domain ID domain_id	2pfdB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	990 — Formiminotransferase-cyclodeaminase; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Formiminotransferase, N-terminal subdomain

Domain ID domain_id	2pfdB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	670 — Formiminotransferase, C-terminal subdomain

Domain ID domain_id	2pfdB03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	680 — Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle

Domain ID domain_id	2pfdC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	990 — Formiminotransferase-cyclodeaminase; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Formiminotransferase, N-terminal subdomain

Domain ID domain_id	2pfdC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	670 — Formiminotransferase, C-terminal subdomain

Domain ID domain_id	2pfdC03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	680 — Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle

Domain ID domain_id	2pfdD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	990 — Formiminotransferase-cyclodeaminase; Chain B, domain 1
Homologous superfamily homologous superfamily	10 — Formiminotransferase, N-terminal subdomain

Domain ID domain_id	2pfdD02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	670 — Formiminotransferase, C-terminal subdomain

Domain ID domain_id	2pfdD03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	680 — Formiminotetrahydrofolate cyclodeaminase monomer, up-and-down helical bundle

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Unit-cell length a length_a	134.848 Å
Unit-cell length b length_b	134.848 Å
Unit-cell length c length_c	156.365 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	16

Space group space_group	P 4
Space-group number int_tables_number	75
Crystal system crystal_system	—

Resolution resolution	3.420 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.2410
R_work r_work	0.2400
R_free r_free	0.2490

Description description	Formimidoyltransferase-cyclodeaminase
Molecular weight formula_weight	59401.5 kDa
EC 编号 ec_number	2.1.2.5, 4.3.1.4
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	16524

Anisotropically refined structure of FTCD

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

Formimidoyltransferase-cyclodeaminase

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

2pfd__assembly_1__model_1

2pfd__assembly_1__model_1 | I(q)

2pfd__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)

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

Anisotropically refined structure of FTCD

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

Formimidoyltransferase-cyclodeaminase

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

2pfd__assembly_1__model_1

2pfd__assembly_1__model_1 | I(q)

2pfd__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

7. Citations (2)