9qc2

BV333 aminotransferase from Streptomyces sp. mutant W89A

Method: X-RAY DIFFRACTION

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

Aspartate aminotransferase family protein

Streptomyces sp. BV333

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	DI(HYDROXYETHYL)ETHER × 11 TRIETHYLENE GLYCOL × 5 1,2-ETHANEDIOL × 47 GLYCEROL × 6 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL × 1 CHLORIDE ION × 5 MAGNESIUM ION × 14 TETRAETHYLENE GLYCOL × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	DI(HYDROXYETHYL)ETHER × 6 TRIETHYLENE GLYCOL × 4 1,2-ETHANEDIOL × 46 GLYCEROL × 5 CHLORIDE ION × 4 MAGNESIUM ION × 13 TETRAETHYLENE GLYCOL × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	A0AA46ZEV9_9ACTN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–458； UniProt 2–459 Author chain B； PDBConstruct 1–458； UniProt 2–459 Author chain C； PDBConstruct 1–458； UniProt 2–459 Author chain D； PDBConstruct 1–458； UniProt 2–459

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	9qc2
Deposition date deposition_date	2025-03-04
Last revision last_revision	2026-03-18
Structure title title	BV333 aminotransferase from Streptomyces sp. mutant W89A
Keywords keywords	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.

9qc2__assembly_1__model_1

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

Download this curve (.dat)

9qc2__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

9qc2__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.55 Å
Rg (electron density)	27.49 Å
Total Rg	28.33 Å
Atom count	7515
Residues	909
Excluded volume	134300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`9qc2__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`9qc2__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 (10)

Entity 1 Entity 1 polymer

Description description	Aspartate aminotransferase family protein
Molecular weight formula_weight	50885.0 kDa
Mutation mutation	W89A
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	16920

GNPIAVSKDLSRTAYDHLWMHFTRMSSYESAPVPTIVRGEGTYIFDDQGRRYLDGLAGLFVVQAGHGRTELAEAASKQAQDLAFFPIASYAHPKAVELAERLAHEAPGDLNKVFFTTGGGEAVETAWKLAKQYFKLTGKPTKHKVISRAVAYHGTPQGALSITGLPALKAPFEPLVPGAHKVPNTNIYRAPLFGDDPEAFGRWAADQIEQQILFEGPETVAAVFLEPVQNAGGCFPPPPGYFQRVREICDQYDVLLVSDEVICAFGRLGTTFACDKFGYVPDMITCAKGMTSGYSPIGACIISDRLAEPFYQGDNTFLHGYTFGGHPVSSAVALANLDIFDREGLNQHVLDNEGTFFATLQKLHDLPIVGDVRGNGFFYGIELVKDKATKETFTEEETERVLYGFLSKALFDNGLYCRADDRGDPVIQLAPPLISDQSTFDEIEGILRTVLTEAWTKLHHH

Source Source

Source organism organism	Streptomyces sp. BV333
NCBI taxonomy ID ncbi_taxonomy_id	2849673
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	17

Entity 3 Entity 3 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 4 Entity 4 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	93

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 6 Entity 6 non-polymer

Description description	2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL
Molecular weight formula_weight	252.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 8 Entity 8 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	27

Entity 9 Entity 9 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1270

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Unit-cell length a length_a	63.825 Å
Unit-cell length b length_b	90.242 Å
Unit-cell length c length_c	99.446 Å
Unit-cell angle α angle_alpha	66.94 °
Unit-cell angle β angle_beta	73.26 °
Unit-cell angle γ angle_gamma	69.64 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.240 Å
Low-resolution limit resolution_low	80.020 Å
R factor r_factor	—
R_work r_work	0.1710
R_free r_free	0.1954

BV333 aminotransferase from Streptomyces sp. mutant W89A

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

Aspartate aminotransferase family 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

9qc2__assembly_1__model_1

9qc2__assembly_1__model_1 | I(q)

9qc2__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 (10)

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 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

7. Citations (1)

BV333 aminotransferase from Streptomyces sp. mutant W89A

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

Aspartate aminotransferase family 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

9qc2__assembly_1__model_1

9qc2__assembly_1__model_1 | I(q)

9qc2__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 (10)

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 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

7. Citations (1)