3csw

Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution

Method: X-RAY DIFFRACTION

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

Putative branched-chain-amino-acid aminotransferase

Thermotoga maritima MSB8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	PYRIDOXAL-5'-PHOSPHATE × 2 UNKNOWN LIGAND × 4 CITRIC ACID × 4 (4S)-2-METHYL-2,4-PENTANEDIOL × 8 CHLORIDE ION × 4 water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	PYRIDOXAL-5'-PHOSPHATE × 2 UNKNOWN LIGAND × 4 CITRIC ACID × 2 (4S)-2-METHYL-2,4-PENTANEDIOL × 6 CHLORIDE ION × 4 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ILVE_THEMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 14–285； UniProt 2–273 Author chain B； PDBConstruct 14–285； UniProt 2–273 Author chain C； PDBConstruct 14–285； UniProt 2–273 Author chain D； PDBConstruct 14–285； UniProt 2–273

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	3csw
Deposition date deposition_date	2008-04-10
Structure title title	Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution
Keywords keywords	;TM0831, Putative Branched-Chain Amino Acid Aminotransferase, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Pyridoxal phosphate, TRANSFERASE ;; TRANSFERASE
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.

3csw__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3csw__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3csw__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	33.79 Å
Rg (electron density)	33.14 Å
Total Rg	33.57 Å
Atom count	8846
Residues	1090
Excluded volume	159120 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3csw__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3csw__assembly_2__model_1`	tetrameric （4）	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 (7)

Entity 1 Entity 1 polymer

Description description	Putative branched-chain-amino-acid aminotransferase
Molecular weight formula_weight	32762.0 kDa
EC 编号 ec_number	2.6.1.42
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	9636

MGSDKIHHHHHHVLIWWRGKFRRADEISLDFSLFEKSLQGAVYETLRTYSRAPFAAYKHYTRLKRSADFFNLPLSLSFDEFTKVLKAGADEFKQEVRIKVYLFPDSGEVLFVFSPLNIPDLETGVEVKISNVRRIPDLSTPPALKITGRTDIVLARREIVDCYDVILLGLNGQVCEGSFSNVFLVKEGKLITPSLDSGILDGITRENVIKLAKSLEIPVEERVVWVWELFEADEMFLTHTSAGVVPVRRLNEHSFFEEEPGPVTATLMENFEPFVLNLEENWVGI

Source Source

Source organism organism	Thermotoga maritima MSB8
NCBI taxonomy ID ncbi_taxonomy_id	243274
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PYRIDOXAL-5'-PHOSPHATE
Molecular weight formula_weight	247.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	UNKNOWN LIGAND
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	CITRIC ACID
Molecular weight formula_weight	192.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 5 Entity 5 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 6 Entity 6 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	621

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3cswa1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.0 — automated matches

Domain ID domain_id	d3cswa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3cswb1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.0 — automated matches

Domain ID domain_id	d3cswb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3cswc1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.0 — automated matches

Domain ID domain_id	d3cswc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3cswd1
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.0 — automated matches

Domain ID domain_id	d3cswd2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (8 domains)

Domain ID domain_id	3cswA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	3cswA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

Domain ID domain_id	3cswB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	3cswB02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

Domain ID domain_id	3cswC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	3cswC02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

Domain ID domain_id	3cswD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	3cswD02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

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Unit-cell length a length_a	107.710 Å
Unit-cell length b length_b	129.760 Å
Unit-cell length c length_c	298.690 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	32

Space group space_group	I 21 21 21
Space-group number int_tables_number	24
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	29.748 Å
R factor r_factor	0.1680
R_work r_work	0.1670
R_free r_free	0.2000

Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution

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

Putative branched-chain-amino-acid aminotransferase

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

3csw__assembly_2__model_1

3csw__assembly_2__model_1 | I(q)

3csw__assembly_2__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 (7)

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 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Crystal structure of a putative branched-chain amino acid aminotransferase (TM0831) from Thermotoga maritima at 2.15 A resolution

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

Putative branched-chain-amino-acid aminotransferase

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

3csw__assembly_2__model_1

3csw__assembly_2__model_1 | I(q)

3csw__assembly_2__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 (7)

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 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)