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Open data
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Basic information
Entry | Database: PDB / ID: 1oaa | ||||||
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Title | MOUSE SEPIAPTERIN REDUCTASE COMPLEXED WITH NADP AND OXALOACETATE | ||||||
![]() | SEPIAPTERIN REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / SEPIAPTERIN REDUCTASE / TETRAHYDROBIOPTERIN | ||||||
Function / homology | ![]() pteridine metabolic process / tetrahydrobiopterin metabolic process / sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) / sepiapterin reductase (NADP+) 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 (NADP+) 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Auerbach, G. / Herrmann, A. / Bacher, A. / Huber, R. | ||||||
![]() | ![]() 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: ![]() Title: The Pathway from GTP to Tetrahydrobiopterin: Three-Dimensional Structures of GTP Cyclohydrolase I and 6-Pyruvoyl Tetrahydropterin Synthase Authors: Auerbach, G. / Nar, H. #2: ![]() Title: 6-Pyruvoyl Tetrahydropterin Synthase, an Enzyme with a Novel Type of Active Site Involving Both Zinc Binding and an Intersubunit Catalytic Triad Motif; Site-Directed Mutagenesis of the ...Title: 6-Pyruvoyl Tetrahydropterin Synthase, an Enzyme with a Novel Type of Active Site Involving Both Zinc Binding and an Intersubunit Catalytic Triad Motif; Site-Directed Mutagenesis of the Proposed Active Center, Characterization of the Metal Binding Site and Modelling of Substrate Binding Authors: Burgisser, D.M. / Thony, B. / Redweik, U. / Hess, D. / Heizmann, C.W. / Huber, R. / Nar, H. #3: ![]() Title: Active Site Topology and Reaction Mechanism of GTP Cyclohydrolase I Authors: Nar, H. / Huber, R. / Auerbach, G. / Fischer, M. / Hosl, C. / Ritz, H. / Bracher, A. / Meining, W. / Eberhardt, S. / Bacher, A. #4: ![]() Title: Atomic Structure of GTP Cyclohydrolase I Authors: Nar, H. / Huber, R. / Meining, W. / Schmid, C. / Weinkauf, S. / Bacher, A. #5: ![]() Title: Three-Dimensional Structure of 6-Pyruvoyl Tetrahydropterin Synthase, an Enzyme Involved in Tetrahydrobiopterin Biosynthesis Authors: Nar, H. / Huber, R. / Heizmann, C.W. / Thony, B. / Burgisser, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 77.1 KB | Display | ![]() |
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PDB format | ![]() | 55.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 484.9 KB | Display | ![]() |
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Full document | ![]() | 488.3 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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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: 27648.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q64105, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) | ||||||
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#2: Chemical | #3: Chemical | ChemComp-OAA / | #4: Chemical | ChemComp-NAP / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: 95 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→8 Å / Num. obs: 112800 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Rmerge(I) obs: 0.068 |
Reflection shell | Resolution: 1.25→1.28 Å / Redundancy: 2.9 % / % possible all: 97.3 |
Reflection | *PLUS Num. measured all: 630228 |
Reflection shell | *PLUS % possible obs: 97.3 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.25→6 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 29 Å2 |