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1kuv

X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition

Method: X-RAY DIFFRACTION Dmax: 56.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Serotonin N-acetyltransferase

Ovis aries

UniProt Q29495

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：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

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 1KUV 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 ligand/ion 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
1KUX X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition Deposited 2002-01-22 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 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 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
1L0C Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase Deposited 2002-02-08 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：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

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1kuv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kuv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kuv
Deposition date deposition_date2002-01-22
Structure title titleX-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition
Keywords keywordsEnzyme-Inhibitor Complex, Bisubstrate Analog, Alternate Conformations, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.51 Å
Radius of gyration Rg (electron density) rg_electron15.09 Å
Forward intensity I(0) i07685760.00
Molecular weight molecular_weight19660.0 kDa
Excluded volume excluded_volume24305 ų
Envelope volume envelope_volume27128 ų
Hydration-shell volume shell_volume14901 ų
Envelope diameter envelope_diameter57.6 Å
Shell Rg shell_rg21.39 Å
Envelope Rg envelope_rg15.60 Å
Shape Rg shape_rg15.09 Å
Total Rg total_rg16.21 Å
Total atoms total_atoms1377
Residues n_residues166
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax56.7 Å
Rg (real space) rg_real16.39 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real7.6860e+06
I(0) uncertainty (real space) i0_real_error8.9620e+04
Rg (reciprocal space) rg_reciprocal16.41 Å
I(0) (reciprocal space) i0_reciprocal7686000.0000
Solution quality estimate total_estimate0.8426
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8 Å
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.4800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2797000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.651; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1kuva_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamilyd.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family familyd.108.1.1 — N-acetyl transferase, NAT

CATH v4.4 (1 domains)

Domain ID domain_id1kuvA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
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8. Citations (1)

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9. Files and Curves (10)