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- PDB-1mut: NMR STUDY OF MUTT ENZYME, A NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mut | ||||||
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Title | NMR STUDY OF MUTT ENZYME, A NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE | ||||||
![]() | NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE | ||||||
![]() | DNA REPAIR | ||||||
Function / homology | ![]() dGDP catabolic process / 8-oxo-dGTP diphosphatase / 8-oxo-GDP phosphatase activity / 8-oxo-dGDP phosphatase activity / dGTP catabolic process / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / nucleotide-excision repair / manganese ion binding / DNA replication ...dGDP catabolic process / 8-oxo-dGTP diphosphatase / 8-oxo-GDP phosphatase activity / 8-oxo-dGDP phosphatase activity / dGTP catabolic process / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / nucleotide-excision repair / manganese ion binding / DNA replication / DNA repair / magnesium ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Abeygunawardana, C. / Weber, D.J. / Gittis, A.G. / Frick, D.N. / Lin, J. / Miller, A.-F. / Bessman, M.J. / Mildvan, A.S. | ||||||
![]() | ![]() Title: Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase. Authors: Abeygunawardana, C. / Weber, D.J. / Gittis, A.G. / Frick, D.N. / Lin, J. / Miller, A.F. / Bessman, M.J. / Mildvan, A.S. #1: ![]() Title: Secondary Structure of the Mutt Enzyme as Determined by NMR Authors: Weber, D.J. / Abeygunawardana, C. / Bessman, M.J. / Mildvan, A.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 612.6 KB | Display | ![]() |
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PDB format | ![]() | 509.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346.9 KB | Display | ![]() |
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Full document | ![]() | 587.6 KB | Display | |
Data in XML | ![]() | 70 KB | Display | |
Data in CIF | ![]() | 94.5 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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NMR ensembles |
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Components
#1: Protein | Mass: 14945.029 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P08337, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 15 |