SAXSdb — 1l0c

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

Serotonin N-acetyltransferase

Ovis aries

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–207	Mutation：Y168F	COT COA-S-ACETYL TRYPTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 2000, MPD, MES pH 6.5, ammonium acetate, magnesium acetate, lithium chloride, spermidine, DTT, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.30 Å R-free 0.246

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 1L0C	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B6B MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM Deposited 1999-01-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–201（174 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.50 Å R-free 0.282
1B6B MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM Deposited 1999-01-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 28–201（174 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 2.50 Å R-free 0.282
1CJW SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG Deposited 1999-04-19	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 30–195（166 aa）	Not recorded	COT COA-S-ACETYL TRYPTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；pH 6.5	Resolution 1.80 Å R-free 0.230
1IB1 CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX Deposited 2001-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 2–201（200 aa） Chain F 2–201（200 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	COT COA-S-ACETYL TRYPTAMINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 4000, magnesium chloride, lithium sulfate, DTT, EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.70 Å R-free 0.228
1IB1 CRYSTAL STRUCTURE OF THE 14-3-3 ZETA:SEROTONIN N-ACETYLTRANSFERASE COMPLEX Deposited 2001-03-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 2–201（200 aa） Chain H 2–201（200 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	COT COA-S-ACETYL TRYPTAMINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 4000, magnesium chloride, lithium sulfate, DTT, EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.70 Å R-free 0.228
1KUV X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition Deposited 2002-01-22	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–207（207 aa）	Mutation：MET substituted by Se-met	MG MAGNESIUM ION × 1 CA5 COA-S-ACETYL 5-BROMOTRYPTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 2000, MPD, ammonium sulfate, MES pH 6.5, magnesium acetate, DTT, spermidine, and lithium chloride. VAPOR DIFFUSION, HANGING DROP at 277K, temperature 277.0K	Resolution 2.00 Å R-free 0.250
1KUX X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition Deposited 2002-01-22	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–207（207 aa）	Mutation：MET substituted by Se-met	CA3 COA-S-TRIMETHYLENE-ACETYL-TRYPTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 2000, MPD, ammonium sulfate, MES pH 6.5, magnesium acetate, DTT, spermidine, and lithium chloride. pH 6.5, VAPOR DIFFUSION, HANGING DROP at 277K, temperature 277.0K	Resolution 1.80 Å R-free 0.225
1KUY X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition Deposited 2002-01-22	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–207（207 aa）	Mutation：MET substituted by Se-met	COT COA-S-ACETYL TRYPTAMINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG 2000, MPD, ammonium sulfate, MES pH 6.5, magnesium acetate, DTT, spermidine, and lithium chloride. VAPOR DIFFUSION, HANGING DROP at 277K, temperature 277.0K	Resolution 2.40 Å R-free 0.276

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SNAT_SHEEP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–207； UniProt 1–207

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	1l0c
Deposition date deposition_date	2002-02-08
Structure title title	Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase
Keywords keywords	Enzyme-inhibitor complex, bisubstrate analog, alternate conformations, 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	16.45 Å
Radius of gyration Rg (electron density) rg_electron	15.03 Å
Forward intensity I(0) i0	7421540.00
Molecular weight molecular_weight	19541.0 kDa
Excluded volume excluded_volume	24253 Å³
Envelope volume envelope_volume	26707 Å³
Hydration-shell volume shell_volume	14768 Å³
Envelope diameter envelope_diameter	54.7 Å
Shell Rg shell_rg	21.30 Å
Envelope Rg envelope_rg	15.49 Å
Shape Rg shape_rg	15.03 Å
Total Rg total_rg	16.13 Å
Total atoms total_atoms	1374
Residues n_residues	166
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	56.1 Å
Rg (real space) rg_real	16.32 Å
Rg uncertainty (real space) rg_real_error	0.26 Å
I(0) (real space) i0_real	7.4220e+06
I(0) uncertainty (real space) i0_real_error	8.4450e+04
Rg (reciprocal space) rg_reciprocal	16.34 Å
I(0) (reciprocal space) i0_reciprocal	7422000.0000
Solution quality estimate total_estimate	0.8441
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.0 Å
Skewness Skewness skewness	0.155
Kurtosis Kurtosis kurtosis	-0.182
Angular range angular_range	— – 0.4850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2370000.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.658; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.996

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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	Serotonin N-acetyltransferase
Molecular weight formula_weight	23095.6 kDa
EC 编号 ec_number	2.3.1.87
Mutation mutation	Y168F
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	1464

MSTPSVHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDEVQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGHSAHLHALAVHRSFRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPFFQRFGFHPAGPCAIVVGSLTFTEMHCSLRGHAALRRNSDR

来源 Source

来源生物 organism	Ovis aries
通用名 common_name	sheep
NCBI Class编号 ncbi_taxonomy_id	9940
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	COA-S-ACETYL TRYPTAMINE
Molecular weight formula_weight	967.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	90

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1l0ca_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamily	d.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family family	d.108.1.1 — N-acetyl transferase, NAT

CATH v4.4 (1 domains)

Domain ID domain_id	1l0cA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

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8. Citations (1)

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Unit-cell length a length_a	53.210 Å
Unit-cell length b length_b	68.681 Å
Unit-cell length c length_c	89.422 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	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1877
R_work r_work	0.1927
R_free r_free	0.2464

fit	/app/data/saxs_computation/l0/1l0c/1l0c.fit
pddf	/app/data/pr_computation/l0/1l0c/1l0c.pr.out
profile	/app/data/saxs_computation/l0/1l0c/1l0c.dat

Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase

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

Serotonin N-acetyltransferase

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