SAXSdb — 9ztc

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

1,3-beta-glucan synthase component FKS1

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–1876	Mutation：S643P	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.50 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 9ZTC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7XE4 structure of a membrane-bound glycosyltransferase Deposited 2022-03-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–1876（1876 aa）	Not recorded	DD9 nonane × 7 D10 DECANE × 6 C14 TETRADECANE × 1 HP6 HEPTANE × 7 D12 DODECANE × 3 XKP (11R,14S)-17-amino-14-hydroxy-8,14-dioxo-9,13,15-trioxa-14lambda~5~-phosphaheptadecan-11-yl decanoate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7YUY Structure of a mutated membrane-bound glycosyltransferase Deposited 2022-08-18	Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–1876（1876 aa）	Mutation：S643P	DD9 nonane × 7 D10 DECANE × 6 C14 TETRADECANE × 1 HP6 HEPTANE × 7 D12 DODECANE × 3 XKP (11R,14S)-17-amino-14-hydroxy-8,14-dioxo-9,13,15-trioxa-14lambda~5~-phosphaheptadecan-11-yl decanoate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8JZN Structure of a fungal 1,3-beta-glucan synthase Deposited 2023-07-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 2 AV0 Lauryl Maltose Neopentyl Glycol × 2 ERG ERGOSTEROL × 14	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.47 Å
8WL6 Structure of 1,3-beta-glucan synthase component FKS1 Deposited 2023-09-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å
8WLA Cryo-EM structure of the beta-1,3-glucan synthase FKS1-Rho1 complex Deposited 2023-09-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–1876（1876 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9PE1 Structure of beta-1,3-glucan synthase in complex with caspofungin, Rho1 and long glucan Deposited 2025-07-01	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1876（1876 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 29 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 UDP URIDINE-5'-DIPHOSPHATE × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 A1CHR (10R,12S)-10,12-dimethyltetradecanoic acid × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
9PE2 Structure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) in complex with short glucan Deposited 2025-07-01	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1876（1876 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 29 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 UDP URIDINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
9PE3 Structure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) at the catalytically relevant ground state Deposited 2025-07-01	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1876（1876 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 Y01 CHOLESTEROL HEMISUCCINATE × 22 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 UDP URIDINE-5'-DIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.26 Å
9PE4 Structure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) at the catalytically less relevant L2 state Deposited 2025-07-01	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–1876（1876 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 7 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 LMN Lauryl Maltose Neopentyl Glycol × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
9PE5 Structure of beta-1,3-glucan synthase from Saccharomyces cerevisiae (ScFks1) at the catalytically less relevant L1 state Deposited 2025-07-01	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 7 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 1 LMN Lauryl Maltose Neopentyl Glycol × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9UTU Structure of Fks1 in complex with YMR295C Deposited 2025-05-05	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–1876（1876 aa）	Not recorded	MG MAGNESIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.72 Å
9UTW Structure of dimeric FKS1 in complex with tRNA Deposited 2025-05-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: pentameric	Chain B 1–1876（1876 aa） Chain H 1–1876（1876 aa）	Not recorded	MG MAGNESIUM ION × 2 DD9 nonane × 8 D10 DECANE × 2 HP6 HEPTANE × 6 XKP (11R,14S)-17-amino-14-hydroxy-8,14-dioxo-9,13,15-trioxa-14lambda~5~-phosphaheptadecan-11-yl decanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 2 PLM PALMITIC ACID × 16 DCR icosanoic acid × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.96 Å
9WY1 Cryo-EM structure of Fks1 in apo state Deposited 2025-09-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 AV0 Lauryl Maltose Neopentyl Glycol × 2 ERG ERGOSTEROL × 13	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.23 Å
9WZU Cryo-EM structure of Fks1 in complex with enfumafungin Deposited 2025-09-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	ERG ERGOSTEROL × 9 A1E06 Enfumafungin × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.97 Å
9WZV Cryo-EM structure of Fks1 with intact active site Deposited 2025-09-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–1876（1876 aa）	Not recorded	ERG ERGOSTEROL × 21 A1E06 Enfumafungin × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.35 Å
9WZX Cryo-EM structure of Fks1 in open state Deposited 2025-09-29	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 1–1876（1876 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.72 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FKS1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–1876； UniProt 1–1876

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	9ztc
Deposition date deposition_date	2025-12-23
Structure title title	Beta-1,3-glucan synthase Fks1 S643P from Saccharomyces Cerevisiae
Keywords keywords	Enzyme, MEMBRANE PROTEIN; MEMBRANE 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	37.84 Å
Radius of gyration Rg (electron density) rg_electron	37.07 Å
Forward intensity I(0) i0	290811000.00
Molecular weight molecular_weight	143520.0 kDa
Excluded volume excluded_volume	181390 Å³
Envelope volume envelope_volume	247300 Å³
Hydration-shell volume shell_volume	55257 Å³
Envelope diameter envelope_diameter	124.8 Å
Shell Rg shell_rg	43.66 Å
Envelope Rg envelope_rg	36.44 Å
Shape Rg shape_rg	37.05 Å
Total Rg total_rg	37.59 Å
Total atoms total_atoms	19414
Residues n_residues	1350
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	123.9 Å
Rg (real space) rg_real	37.79 Å
Rg uncertainty (real space) rg_real_error	0.76 Å
I(0) (real space) i0_real	2.9080e+08
I(0) uncertainty (real space) i0_real_error	4.3420e+06
Rg (reciprocal space) rg_reciprocal	37.82 Å
I(0) (reciprocal space) i0_reciprocal	290800000.0000
Solution quality estimate total_estimate	0.8952
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	44.2 Å
Skewness Skewness skewness	0.277
Kurtosis Kurtosis kurtosis	-0.491
Angular range angular_range	— – 0.2100 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	43110000.0000
Real-space data points n_real_points	43
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.898

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	1,3-beta-glucan synthase component FKS1
Molecular weight formula_weight	221262.5 kDa
EC 编号 ec_number	2.4.1.34
Mutation mutation	S643P
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	19414

MNTDQQPYQGQTDYTQGPGNGQSQEQDYDQYGQPLYPSQADGYYDPNVAAGTEADMYGQQPPNESYDQDYTNGEYYGQPPNMAAQDGENFSDFSSYGPPGTPGYDSYGGQYTASQMSYGEPNSSGTSTPIYGNYDPNAIAMALPNEPYPAWTADSQSPVSIEQIEDIFIDLTNRLGFQRDSMRNMFDHFMVLLDSRSSRMSPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMSLGKLSRKARKAKKKNKKAMEEANPEDTEETLNKIEGDNSLEAADFRWKAKMNQLSPLERVRHIALYLLCWGEANQVRFTAECLCFIYKCALDYLDSPLCQQRQEPMPEGDFLNRVITPIYHFIRNQVYEIVDGRFVKRERDHNKIVGYDDLNQLFWYPEGIAKIVLEDGTKLIELPLEERYLRLGDVVWDDVFFKTYKETRTWLHLVTNFNRIWVMHISIFWMYFAYNSPTFYTHNYQQLVDNQPLAAYKWASCALGGTVASLIQIVATLCEWSFVPRKWAGAQHLSRRFWFLCIIFGINLGPIIFVFAYDKDTVYSTAAHVVAAVMFFVAVATIIFFSIMPLGGLFTSYMKKSTRRYVASQTFTAAFAPLHGLDRWMSYLVWVTVFAAKYSESYYFLVLPLRDPIRILSTTAMRCTGEYWWGAVLCKVQPKIVLGLVIATDFILFFLDTYLWYIIVNTIFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYEGNENEAEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLTEGEEPRIYSALIDGHCEILDNGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEQVNPYAPGLRYEEQTTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLSQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAMLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLSSLAHESIMCIYDRNKPKTDVLVPIGCYNFQPAVDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFCHLLSLSPMFEVFAGQIYSSALLSDLAIGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSSLIFAPFVFNPHQFAWEDFFLDYRDYIRWLSRGNNQYHRNSWIGYVRMSRARITGFKRKLVGDESEKAAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIAVNLGVLFFCMGMSCCSGPLFGMCCKKTGSVMAGIAHGVAVIVHIAFFIVMWVLESFNFVRMLIGVVTCIQCQRLIFHCMTALMLTREFKNDHANTAFWTGKWYGKGMGYMAWTQPSRELTAKVIELSEFAADFVLGHVILICQLPLIIIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQTRLRKRMVKKYCSLYFLVLAIFAGCIIGPAVASAKIHKHIGDSLDGVVHNLFQPINTTNNDTGSQMSTYQSHYYTHTPSLKTWSTIKLEVLFQGPAAAGSAGSAAGSGEFDYKDHDGDYKDHDIDYKDDDDKHHHHHHHHHH

Entity 2 Entity 2 branched

Description description	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	586.5 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CHOLESTEROL HEMISUCCINATE
Molecular weight formula_weight	486.7 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	3.500 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	194636

fit	/app/data/saxs_computation/zt/9ztc/9ztc.fit
pddf	/app/data/pr_computation/zt/9ztc/9ztc.pr.out
profile	/app/data/saxs_computation/zt/9ztc/9ztc.dat

Beta-1,3-glucan synthase Fks1 S643P from Saccharomyces Cerevisiae

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

1,3-beta-glucan synthase component FKS1

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

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 branched

Entity 3 Entity 3 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)