+Open data
-Basic information
Entry | Database: PDB / ID: 1sep | |||||||||
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Title | MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND SEPIAPTERIN | |||||||||
Components | SEPIAPTERIN REDUCTASE | |||||||||
Keywords | OXIDOREDUCTASE / SEPIAPTERIN REDUCTASE / 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 / protein homodimerization activity / mitochondrion Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 1.95 Å | |||||||||
Authors | Auerbach, G. / Herrmann, A. / Guetlich, M. / Fischer, M. / Jacob, U. / 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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sep.cif.gz | 73.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sep.ent.gz | 53.9 KB | Display | PDB format |
PDBx/mmJSON format | 1sep.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/se/1sep ftp://data.pdbj.org/pub/pdb/validation_reports/se/1sep | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 27908.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Organ: BRAIN / Cellular location (production host): CYTOSOL / Production host: Escherichia coli (E. coli) References: UniProt: Q64105, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-BIO / |
#4: 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 | *PLUS Temperature: 4 ℃ / pH: 6.5 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→8 Å / Num. obs: 31227 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 9.8 % / Rmerge(I) obs: 0.099 |
Reflection shell | Resolution: 1.94→1.95 Å / Redundancy: 8.6 % / % possible all: 96.4 |
Reflection | *PLUS Num. measured all: 304866 |
Reflection shell | *PLUS % possible obs: 96.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 1.95→8 Å / Cross valid method: FREE-R / σ(F): 0 /
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Displacement parameters | Biso mean: 24.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.176 / Rfactor Rfree: 0.216 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |