SAXSdb — 1d6h

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

CHALCONE SYNTHASE

Medicago sativa

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 3–389	Mutation：N336A Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2 COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.15 Å R-free 0.257

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 1D6H	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BI5 CHALCONE SYNTHASE FROM ALFALFA Deposited 1998-06-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.56 Å R-free 0.193
1BQ6 CHALCONE SYNTHASE FROM ALFALFA WITH COENZYME A Deposited 1998-08-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–389（388 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2 COA COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.56 Å R-free 0.212
1CGK CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH NARINGENIN Deposited 1999-03-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Not recorded	NAR NARINGENIN × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；THE DROPLE CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5) , IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES 16 MM NARINGENIN PRIOR TO FREEZING AT 105 K, pH 6.50	Resolution 1.84 Å R-free 0.225
1CGZ CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH RESVERATROL Deposited 1999-03-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Not recorded	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 1.70 Å R-free 0.217
1CHW CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH HEXANOYL-COA Deposited 1999-03-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：C164S Mutation：C164S	HXC HEXANOYL-COENZYME A × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；THE CRYSTALS WERE OBTAINED OVERNIGHT AT 4 C HANGING-DROP VAPOR DIFFUSION METHOD. THE DROPLET CONSISTED ON 25 MGR/ML (FINAL CONCENTRATION) PROTEIN MIXED WITH THE RESERVOIR WHICH CONTAINED 2.4 M AMMONIUM SULFATE, 100 MM PIPES BUFFER (PH 6.5), IN THE PRESENCE (UP TO 5 MM) OR ABSENCE OF DTT REDUCING AGENT. CRYSTALS WERE STABILIZED IN 40% (V/V) PEG400, 100 MM PIPES AND 20 MM HEXANOYL-COA PRIOR TO FREEZING AT 105 K.	Resolution 1.90 Å R-free 0.290
1CML CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA Deposited 1999-03-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：C164A	SO4 SULFATE ION × 2 MLC MALONYL-COENZYME A × 2 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.50	Resolution 1.69 Å R-free 0.200
1D6F CHALCONE SYNTHASE C164A MUTANT Deposited 1999-10-13	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：C164A	SO4 SULFATE ION × 2 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.69 Å R-free 0.201
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–389（388 aa） Fragment：CHS Chain B 2–389（388 aa） Fragment：CHS	Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.269
1D6I CHALCONE SYNTHASE (H303Q MUTANT) Deposited 1999-10-13	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–389（388 aa） Fragment：CHS Chain B 2–389（388 aa） Fragment：CHS	Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：H303Q Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M AMMONIUM SULFATE, 0.1 M BIS-TRIS PROPANE, 2 MM DITHIOTHREITOL (DTT), pH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 2.00 Å R-free 0.269
1I86 CHALCONE SYNTHASE, G256A MUTANT Deposited 2001-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：CHALCONE SYNTHASE (G256A) Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 100 mM PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.50 Å R-free 0.221
1I88 CHALCONE SYNTHASE (G256V) Deposited 2001-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256V Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.45 Å R-free 0.221
1I89 Chalcone synthase (G256L) Deposited 2001-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：G256L Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256L Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.86 Å R-free 0.259
1I8B Chalcone synthase (G256F) Deposited 2001-03-12	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：G256F Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；2.2-2.4 M ammonium sulfate, 0.1 M PIPES, 5 mM DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.95 Å R-free 0.251
1JWX Chalcone Synthase--F215S mutant Deposited 2001-09-05	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa）	Mutation：F215S Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；ammonium sulfate, PIPES, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.63 Å R-free 0.225
1U0V An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization of Specificity of Type III Polyketide Synthases: 18xCHS structure Deposited 2004-07-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 1.90 Å R-free 0.227
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–389（389 aa） Chain B 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.264
1U0W An Aldol Switch Discovered in Stilbene Synthases Mediates Cyclization Specificity of Type III Polyketide Synthases: 18xCHS+resveratrol Structure Deposited 2004-07-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–389（389 aa） Chain D 1–389（389 aa）	Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D Mutation：D96A, V98L, V99A, V100M, T131S, S133T, G134T, V135P, M137L, Y157V, M158G, M159V, Y160F, Q161H, L268K, K269G, D270A, G273D	STL RESVERATROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 8000, ammonium acetate, HEPES-Na+ buffer, ethylene glycol, resveratrol, DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.00 Å R-free 0.264

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CHS2_MEDSA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–387； UniProt 3–389

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	1d6h
Deposition date deposition_date	1999-10-13
Structure title title	CHALONE SYNTHASE (N336A MUTANT COMPLEXED WITH COA)
Keywords keywords	POLYPETIDE SYNTHASE, FLAVONOID BIOSYNTHESIS, MALONYL-COA DECARBOXYLATION, SITE-DIRECTED MUTANT, TRANSFERASE; TRANSFERASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	22.19 Å
Radius of gyration Rg (electron density) rg_electron	21.04 Å
Forward intensity I(0) i0	31572000.00
Molecular weight molecular_weight	43326.0 kDa
Excluded volume excluded_volume	54316 Å³
Envelope volume envelope_volume	62519 Å³
Hydration-shell volume shell_volume	24402 Å³
Envelope diameter envelope_diameter	80.7 Å
Shell Rg shell_rg	28.31 Å
Envelope Rg envelope_rg	21.57 Å
Shape Rg shape_rg	21.03 Å
Total Rg total_rg	21.96 Å
Total atoms total_atoms	3032
Residues n_residues	386
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	80.1 Å
Rg (real space) rg_real	22.14 Å
Rg uncertainty (real space) rg_real_error	0.68 Å
I(0) (real space) i0_real	3.1570e+07
I(0) uncertainty (real space) i0_real_error	4.4280e+05
Rg (reciprocal space) rg_reciprocal	22.15 Å
I(0) (reciprocal space) i0_reciprocal	31570000.0000
Solution quality estimate total_estimate	0.8358
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.1 Å
Skewness Skewness skewness	0.354
Kurtosis Kurtosis kurtosis	-0.116
Angular range angular_range	— – 0.3600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7167000.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.652; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.974

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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	CHALCONE SYNTHASE
Molecular weight formula_weight	42513.9 kDa
EC 编号 ec_number	2.3.1.74
Mutation mutation	N336A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3224

SVSEIRKAQRAEGPATILAIGTANPANCVEQSTYPDFYFKITNSEHKTELKEKFQRMCDKSMIKRRYMYLTEEILKENPNVCEYMAPSLDARQDMVVVEVPRLGKEAAVKAIKEWGQPKSKITHLIVCTTSGVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVWTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNITKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMNATREVLSEYGAMSSACVLFILDEMRKKSTQNGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVAI

来源 Source

来源生物 organism	Medicago sativa
NCBI Class编号 ncbi_taxonomy_id	3879
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	COENZYME A
Molecular weight formula_weight	767.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	184

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1d6ha1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

Domain ID domain_id	d1d6ha2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.95 — Thiolase-like
Superfamily Superfamily superfamily	c.95.1 — Thiolase-like
Family Family family	c.95.1.2 — Chalcone synthase-like

CATH v4.4 (2 domains)

Domain ID domain_id	1d6hA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

Domain ID domain_id	1d6hA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	47 — Peroxisomal Thiolase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Thiolase/Chalcone synthase

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8. Citations (1)

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Unit-cell length a length_a	97.361 Å
Unit-cell length b length_b	97.361 Å
Unit-cell length c length_c	65.207 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	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	85.000 Å
R factor r_factor	—
R_work r_work	0.1842
R_free r_free	0.2574

fit	/app/data/saxs_computation/d6/1d6h/1d6h.fit
pddf	/app/data/pr_computation/d6/1d6h/1d6h.pr.out
profile	/app/data/saxs_computation/d6/1d6h/1d6h.dat

CHALONE SYNTHASE (N336A MUTANT COMPLEXED WITH COA)

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

CHALCONE 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

Diffraction experiment Diffraction