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1b6b

MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM

Method: X-RAY DIFFRACTION Dmax: 71.7 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (ARYLALKYLAMINE 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 28–201 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5 Resolution 2.50 Å R-free 0.282
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 28–201 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5 Resolution 2.50 Å R-free 0.282

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 1B6B Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CJW SEROTONIN N-ACETYLTRANSFERASE COMPLEXED WITH A BISUBSTRATE ANALOG Deposited 1999-04-19 Different construct Different ligand/ion 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 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 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 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 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 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 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 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 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 7 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 1–174； UniProt 28–201 Author chain B； PDBConstruct 1–174； UniProt 28–201

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 1b6b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b6b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b6b
Deposition date deposition_date1999-01-13
Structure title titleMELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM
Keywords keywordsACETYLTRANSFERASE, 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_guinier22.82 Å
Radius of gyration Rg (electron density) rg_electron21.97 Å
Forward intensity I(0) i021489000.00
Molecular weight molecular_weight34972.0 kDa
Excluded volume excluded_volume43654 ų
Envelope volume envelope_volume53400 ų
Hydration-shell volume shell_volume20845 ų
Envelope diameter envelope_diameter72.3 Å
Shell Rg shell_rg27.83 Å
Envelope Rg envelope_rg22.04 Å
Shape Rg shape_rg21.96 Å
Total Rg total_rg22.79 Å
Total atoms total_atoms2471
Residues n_residues324
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 dmax71.7 Å
Rg (real space) rg_real22.83 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real2.1490e+07
I(0) uncertainty (real space) i0_real_error2.9640e+05
Rg (reciprocal space) rg_reciprocal22.83 Å
I(0) (reciprocal space) i0_reciprocal21490000.0000
Solution quality estimate total_estimate0.9025
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0 Å
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.3500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4277000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.987
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1b6ba_
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
Domain ID domain_idd1b6bb_
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 (2 domains)

Domain ID domain_id1b6bA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily30 — Gcn5-related N-acetyltransferase (GNAT)
Domain ID domain_id1b6bB00
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)