SAXSdb — 2vjo

▼

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

FORMYL-COENZYME A TRANSFERASE

OXALOBACTER FORMIGENES

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	COENZYME A × 2 CHLORIDE ION × 2 OXALATE ION × 1 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FCTA_OXAFO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–428； UniProt 1–428 Author chain B； PDBConstruct 1–428； UniProt 1–428

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2vjo
Deposition date deposition_date	2007-12-11
Structure title title	Formyl-CoA transferase mutant variant Q17A with aspartyl-CoA thioester intermediates and oxalate
Keywords keywords	CYTOPLASM, TRANSFERASE, CLASS III COA TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

2vjo__assembly_1__model_1

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

Download this curve (.dat)

2vjo__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2vjo__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.78 Å
Rg (electron density)	26.82 Å
Total Rg	27.52 Å
Atom count	6735
Residues	854
Excluded volume	119420 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2vjo__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	FORMYL-COENZYME A TRANSFERASE
Molecular weight formula_weight	47305.8 kDa
EC 编号 ec_number	2.8.3.16
Mutation mutation	YES
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	7210

MTKPLDGINVLDFTHVAAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQDKPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGALDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAATTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEIRHKTGRGQKVAVAMQDAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSVPRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEWKDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVMSMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLLGEHTDEVLKELGLDDAKIKELHAKQVV

Source Source

Source organism organism	OXALOBACTER FORMIGENES
NCBI taxonomy ID ncbi_taxonomy_id	847
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	COENZYME A
Molecular weight formula_weight	767.5 kDa
Source method src_method	syn
Copy count entity_count	2

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	OXALATE ION
Molecular weight formula_weight	88.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
Molecular weight formula_weight	238.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	440

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2vjoa_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

Domain ID domain_id	d2vjob_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.123 — CoA-transferase family III (CaiB/BaiF)
Superfamily Superfamily superfamily	c.123.1 — CoA-transferase family III (CaiB/BaiF)
Family Family family	c.123.1.1 — CoA-transferase family III (CaiB/BaiF)

CATH v4.4 (4 domains)

Domain ID domain_id	2vjoA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	2vjoA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

Domain ID domain_id	2vjoB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	10540 — Crotonobetainyl-coa:carnitine coa-transferase; domain 1

Domain ID domain_id	2vjoB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	1540 — formyl-coa transferase, domain 3
Homologous superfamily homologous superfamily	10 — formyl-coa transferase, domain 3

▶

Unit-cell length a length_a	153.593 Å
Unit-cell length b length_b	153.593 Å
Unit-cell length c length_c	98.055 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	I 4
Space-group number int_tables_number	79
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2080
R_work r_work	0.2060
R_free r_free	0.2480

Formyl-CoA transferase mutant variant Q17A with aspartyl-CoA thioester intermediates and oxalate

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

FORMYL-COENZYME A TRANSFERASE

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

2vjo__assembly_1__model_1

2vjo__assembly_1__model_1 | I(q)

2vjo__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)

Formyl-CoA transferase mutant variant Q17A with aspartyl-CoA thioester intermediates and oxalate

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

FORMYL-COENZYME A TRANSFERASE

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

2vjo__assembly_1__model_1

2vjo__assembly_1__model_1 | I(q)

2vjo__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (1)