SAXSdb — 4gxq

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

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

Burkholderia xenovorans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count
2	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count
3	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q13WK3_BURXL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 444–468； UniProt 473–497 Author chain B； PDBConstruct 444–468； UniProt 473–497 Author chain C； PDBConstruct 444–468； UniProt 473–497

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

Burkholderia xenovorans

UniProt Q6ND88

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count
2	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count
3	Insufficient information	Monomer	Protein 1	ADENOSINE-5'-TRIPHOSPHATE × 1 MAGNESIUM ION × 1 CARBONATE ION × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6ND88_RHOPA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–443； UniProt 1–443 Author chain A； PDBConstruct 469–506； UniProt 466–503 Author chain B； PDBConstruct 1–443； UniProt 1–443 Author chain B； PDBConstruct 469–506； UniProt 466–503 Author chain C； PDBConstruct 1–443； UniProt 1–443 Author chain C； PDBConstruct 469–506； UniProt 466–503

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	4gxq
Deposition date deposition_date	2012-09-04
Structure title title	Crystal Structure of ATP bound RpMatB-BxBclM chimera B1
Keywords keywords	RpMatB-BxBclM chimera, ANL Superfamily, methylmalonate-CoA ligase, malonate-CoA ligase, methylmalonate, malonate, 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.

4gxq__assembly_1__model_1

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

Download this curve (.dat)

4gxq__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4gxq__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.18 Å
Rg (electron density)	23.32 Å
Total Rg	24.23 Å
Atom count	3972
Residues	476
Excluded volume	71384 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4gxq__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4gxq__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`4gxq__assembly_3__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 (5)

Entity 1 Entity 1 polymer

Description description	Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein
Molecular weight formula_weight	55892.2 kDa
EC 编号 ec_number	6.2.1.-
Mutation mutation	K491A
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	13557

MNANLFARLFDKLDDPHKLAIETAAGDKISYAELVARAGRVANVLVARGLQVGDRVAAQTEKSVEALVLYLATVRAGGVYLPLNTAYTLHELDYFITDAEPKIVVCDPSKRDGIAAIAAKVGATVETLGPDGRGSLTDAAAGASEAFATIDRGADDLAAILYTSGTTGRSKGAMLSHDNLASNSLTLVDYWRFTPDDVLIHALPIYHTHGLFVASNVTLFARGSMIFLPKFDPDKILDLMARATVLMGVPTFYTRLLQSPRLTKETTGHMRLFISGSAPLLADTHREWSAKTGHAVLERYGMTETNMNTSNPYDGDRVPGAVGPALPGVSARVTDPETGKELPRGDIGMIEVKGPNVFKGYWRMPEKTKSEFRDDGFFITGDLGKIDERGYVHILGRGKDLVITGGFNVYPKEIESEIDAMPGVVESAVIGVPHADFGEGVTAFVVLKREFAPSEILAEELKAFVKDRLAKFKMPKKVIFVDDLPRNTMGAVQKNVLRETYKDIYK

Source Source

Source organism organism	Burkholderia xenovorans
NCBI taxonomy ID ncbi_taxonomy_id	266265
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	ADENOSINE-5'-TRIPHOSPHATE
Molecular weight formula_weight	507.2 kDa
Source method src_method	syn
Copy count entity_count	3

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	3

Entity 4 Entity 4 non-polymer

Description description	CARBONATE ION
Molecular weight formula_weight	60.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1586

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d4gxqa_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.23 — Acetyl-CoA synthetase-like
Superfamily Superfamily superfamily	e.23.1 — Acetyl-CoA synthetase-like
Family Family family	e.23.1.0 — automated matches

Domain ID domain_id	d4gxqb_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.23 — Acetyl-CoA synthetase-like
Superfamily Superfamily superfamily	e.23.1 — Acetyl-CoA synthetase-like
Family Family family	e.23.1.0 — automated matches

Domain ID domain_id	d4gxqc_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.23 — Acetyl-CoA synthetase-like
Superfamily Superfamily superfamily	e.23.1 — Acetyl-CoA synthetase-like
Family Family family	e.23.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id	4gxqA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	12780 — ANL, N-terminal domain

Domain ID domain_id	4gxqA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	30 — ANL, C-terminal domain

Domain ID domain_id	4gxqB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	12780 — ANL, N-terminal domain

Domain ID domain_id	4gxqB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	30 — ANL, C-terminal domain

Domain ID domain_id	4gxqC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	12780 — ANL, N-terminal domain

Domain ID domain_id	4gxqC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	300 — GMP Synthetase; Chain A, domain 3
Homologous superfamily homologous superfamily	30 — ANL, C-terminal domain

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Unit-cell length a length_a	299.305 Å
Unit-cell length b length_b	299.305 Å
Unit-cell length c length_c	47.909 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	18

Space group space_group	P 61
Space-group number int_tables_number	169
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	24.950 Å
R factor r_factor	0.2206
R_work r_work	0.2188
R_free r_free	0.2544

Crystal Structure of ATP bound RpMatB-BxBclM chimera B1

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

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

State in the Current Structure

Other States of the Same Protein in the Database

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

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

4gxq__assembly_1__model_1

4gxq__assembly_1__model_1 | I(q)

4gxq__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Crystal Structure of ATP bound RpMatB-BxBclM chimera B1

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

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Malonyl CoA synthetase, Benzoate-CoA ligase Chimeric protein

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

4gxq__assembly_1__model_1

4gxq__assembly_1__model_1 | I(q)

4gxq__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

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)