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- PDB-1b6b: MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSF... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1b6b | ||||||
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Title | MELATONIN BIOSYNTHESIS: THE STRUCTURE OF SEROTONIN N-ACETYLTRANSFERASE AT 2.5 A RESOLUTION SUGGESTS A CATALYTIC MECHANISM | ||||||
![]() | PROTEIN (ARYLALKYLAMINE N-ACETYLTRANSFERASE) | ||||||
![]() | TRANSFERASE / ACETYLTRANSFERASE | ||||||
Function / homology | ![]() aralkylamine N-acetyltransferase / aralkylamine N-acetyltransferase activity / melatonin biosynthetic process / N-terminal protein amino acid acetylation / response to light stimulus / cellular response to cAMP / circadian rhythm / perinuclear region of cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hickman, A.B. / Klein, D.C. / Dyda, F. | ||||||
![]() | ![]() Title: Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism. Authors: Hickman, A.B. / Klein, D.C. / Dyda, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.4 KB | Display | ![]() |
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PDB format | ![]() | 57 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.4 KB | Display | ![]() |
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Full document | ![]() | 428.6 KB | Display | |
Data in XML | ![]() | 15.8 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.8237, -0.5629, -0.0681), Vector: |
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Components
#1: Protein | Mass: 19556.477 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q29495, aralkylamine N-acetyltransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 49 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: microdialysis | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K | ||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 15, 1998 / Details: MIRROR | ||||||||||||
Radiation | Monochromator: SI111 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 3→20 Å / Num. obs: 6476 / % possible obs: 85.4 % / Observed criterion σ(I): 0 / Redundancy: 5 % / Rsym value: 6.3 / Net I/σ(I): 14.5 | ||||||||||||
Reflection shell | Resolution: 3→3.11 Å / Redundancy: 3 % / Mean I/σ(I) obs: 10.5 / Rsym value: 13.2 / % possible all: 93.2 | ||||||||||||
Reflection | *PLUS Num. measured all: 39960 / Rmerge(I) obs: 0.063 | ||||||||||||
Reflection shell | *PLUS % possible obs: 93.2 % / Rmerge(I) obs: 0.132 |
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Processing
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Refinement | Method to determine structure: ![]() Details: IN STRUCTURE DETERMINATION, A TRUNCATED CONSTRUCT WAS USED BETWEEN RESIDUES 27 - 201
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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