SAXSdb — 9yjz

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

Acetolactate synthase

Aspergillus fumigatus

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 112–752 Chain B； UniProt 112–752	Not recorded	MG MAGNESIUM ION × 2 TPP THIAMINE DIPHOSPHATE × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.76 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9YJZ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9YK0 cryoEM structure of Aspergillus fumigatus acetolactate synthase (ALS) in complex with a novel inhibitor Deposited 2025-10-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 112–752（641 aa） Chain B 112–752（641 aa）	Not recorded	MG MAGNESIUM ION × 2 TPP THIAMINE DIPHOSPHATE × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 A1CXH (1R,2R,4aR,8R,8aR)-8-[(3S,5R)-5-(3-hydroxypropyl)-2,4-dioxopyrrolidin-3-yl]-3,8-dimethyl-2-propyl-1,2,4a,5,6,7,8,8a-octahydronaphthalene-1-carbaldehyde × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.36 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	B0XXW9_ASPFC
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–641； UniProt 112–752 Author chain B； PDBConstruct 1–641； UniProt 112–752

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	9yjz
Deposition date deposition_date	2025-10-06
Structure title title	cryoEM structure of Apo Aspergillus fumigatus acetolactate synthase (ALS)
Keywords keywords	Branched-Chain Amino Acid Synthesis, antifungal target, herbicide target, anti fugal infection, PLANT PROTEIN; PLANT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	32.32 Å
Radius of gyration Rg (electron density) rg_electron	31.96 Å
Forward intensity I(0) i0	261559000.00
Molecular weight molecular_weight	129960.0 kDa
Excluded volume excluded_volume	162700 Å³
Envelope volume envelope_volume	194220 Å³
Hydration-shell volume shell_volume	49464 Å³
Envelope diameter envelope_diameter	117.3 Å
Shell Rg shell_rg	39.94 Å
Envelope Rg envelope_rg	32.32 Å
Shape Rg shape_rg	31.97 Å
Total Rg total_rg	32.48 Å
Total atoms total_atoms	9216
Residues n_residues	1164
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	109.6 Å
Rg (real space) rg_real	32.32 Å
Rg uncertainty (real space) rg_real_error	0.72 Å
I(0) (real space) i0_real	2.6160e+08
I(0) uncertainty (real space) i0_real_error	4.2430e+06
Rg (reciprocal space) rg_reciprocal	32.32 Å
I(0) (reciprocal space) i0_reciprocal	261600000.0000
Solution quality estimate total_estimate	0.8684
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.0 Å
Skewness Skewness skewness	0.424
Kurtosis Kurtosis kurtosis	-0.160
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	240700000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.785; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Acetolactate synthase
Molecular weight formula_weight	70307.8 kDa
EC 编号 ec_number	2.2.1.6
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	9216

SPAFNQEPHRNEVSPLQNRHLPELDDSTSLITVMSRFVGLSGGQIFHEMMLRLGVKHIFGYPGGAILPVFDAIYNSKHFDFVLPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMQDALSDGTPMVVFCGQVPTSSIGTDSFQEADVVGISRACTKWNVMVKSVAELPRRIQEAFEIATSGRPGPVLVDLPKDITAGILRKPIPMNSTIPSLPSAATMAARELSMKQLESSIDRVARLVNIAQKPVLYVGQGLLARPDGPKVLKELADKACIPVTTTLQGLGGFDELDPKALHMLGMHGSAYANMAMQEADLIIAVGARFDDRVTGNLSKFAPQAKLAASEKRGGIVHFEIMPKNINKVVQANEAVEGDCAENIRLLLPHVKPVSERPEWFAQINDWKARFPFSLYEKQSPEGPIKPQALIEKLSDLTAPIKDRTIITTGVGQHQMWAAQHFRWRHPRTMITSGGLGTMGYGLPAAIGAKVARPDCLVIDIDGDASFNMTLTELTTAAQFNIGVKVLLLNNEEQGMVTQWQNLFYEDRYSHTHQKNPDFVPMARSMGVAAERCTKPSEVEEKLKWLIESDGPALLEVFTDRKVPVLPMVPAGSALHEFLVYDEAKEKERKALLRSRTAPEYLHK

来源 Source

来源生物 organism	Aspergillus fumigatus
NCBI Class编号 ncbi_taxonomy_id	746128
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	THIAMINE DIPHOSPHATE
Molecular weight formula_weight	425.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	2.760 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	2.76 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	64577

fit	/app/data/saxs_computation/yj/9yjz/9yjz.fit
pddf	/app/data/pr_computation/yj/9yjz/9yjz.pr.out
profile	/app/data/saxs_computation/yj/9yjz/9yjz.dat

cryoEM structure of Apo Aspergillus fumigatus acetolactate synthase (ALS)

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

Acetolactate synthase

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D