+Open data
-Basic information
Entry | Database: PDB / ID: 1nas | ||||||
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Title | SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN | ||||||
Components | SEPIAPTERIN REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / SEPIAPTERIN REDUCTASE / SHORT-CHAIN DEHYDROGENASE / SDR FAMILY / N-ACETYL SEROTONIN / TETRAHYDROBIOPTERIN | ||||||
Function / homology | Function and homology information pteridine metabolic process / tetrahydrobiopterin metabolic process / sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) / sepiapterin reductase activity / L-phenylalanine metabolic process / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / cell morphogenesis involved in neuron differentiation / voluntary musculoskeletal movement / serotonin metabolic process ...pteridine metabolic process / tetrahydrobiopterin metabolic process / sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) / sepiapterin reductase activity / L-phenylalanine metabolic process / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / cell morphogenesis involved in neuron differentiation / voluntary musculoskeletal movement / serotonin metabolic process / tetrahydrobiopterin biosynthetic process / norepinephrine metabolic process / dopamine metabolic process / regulation of multicellular organism growth / nitric oxide biosynthetic process / protein homodimerization activity / mitochondrion / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Auerbach, G. / Herrmann, A. / Bacher, A. / Huber, R. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. Authors: Auerbach, G. / Herrmann, A. / Gutlich, M. / Fischer, M. / Jacob, U. / Bacher, A. / Huber, R. #1: Journal: Biol.Chem. / Year: 1997 Title: The Pathway from GTP to Tetrahydrobiopterin: Three-Dimensional Structures of GTP Cyclohydrolase I and 6-Pyruvoyl Tetrahydropterin Synthase Authors: Auerbach, G. / Nar, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nas.cif.gz | 74.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nas.ent.gz | 54.2 KB | Display | PDB format |
PDBx/mmJSON format | 1nas.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/1nas ftp://data.pdbj.org/pub/pdb/validation_reports/na/1nas | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 27648.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Organ: BRAIN / Production host: Escherichia coli (E. coli) References: UniProt: Q64105, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) |
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#2: Chemical | ChemComp-OAA / |
#3: Chemical | ChemComp-NAP / |
#4: Chemical | ChemComp-ASE / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 66 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.7 / Details: pH 4.7 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.5 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 280 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Date: Oct 23, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→25 Å / Num. obs: 23193 / % possible obs: 93.2 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Num. measured all: 167681 / Rmerge(I) obs: 0.061 |
Reflection shell | *PLUS % possible obs: 88.4 % |
-Processing
Software |
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Refinement | Resolution: 2.1→8 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 20.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refine LS restraints |
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Software | *PLUS Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |