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- PDB-1gzu: Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltr... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gzu | |||||||||
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Title | Crystal Structure of Human Nicotinamide Mononucleotide Adenylyltransferase in Complex with NMN | |||||||||
![]() | NICOTINAMIDE MONONUCLEOTIDE ADENYLYL TRANSFERASE | |||||||||
![]() | TRANSFERASE / NAD BIOSYNTHESIS / ADENYLYLTRANSFERASE | |||||||||
Function / homology | ![]() negative regulation of apoptotic DNA fragmentation / protein ADP-ribosyltransferase-substrate adaptor activity / nicotinamide-nucleotide adenylyltransferase / nicotinamide-nucleotide adenylyltransferase activity / nicotinate-nucleotide adenylyltransferase / nucleotide biosynthetic process / nicotinate-nucleotide adenylyltransferase activity / Nicotinate metabolism / ATP generation from poly-ADP-D-ribose / NAD biosynthetic process ...negative regulation of apoptotic DNA fragmentation / protein ADP-ribosyltransferase-substrate adaptor activity / nicotinamide-nucleotide adenylyltransferase / nicotinamide-nucleotide adenylyltransferase activity / nicotinate-nucleotide adenylyltransferase / nucleotide biosynthetic process / nicotinate-nucleotide adenylyltransferase activity / Nicotinate metabolism / ATP generation from poly-ADP-D-ribose / NAD biosynthetic process / response to wounding / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / nuclear body / negative regulation of DNA-templated transcription / chromatin / nucleoplasm / ATP binding / identical protein binding / nucleus Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Werner, E. / Ziegler, M. / Lerner, F. / Schweiger, M. / Heinemann, U. | |||||||||
![]() | ![]() Title: Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN. Authors: Werner, E. / Ziegler, M. / Lerner, F. / Schweiger, M. / Heinemann, U. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146.9 KB | Display | ![]() |
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PDB format | ![]() | 122.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 556 KB | Display | ![]() |
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Full document | ![]() | 612.9 KB | Display | |
Data in XML | ![]() | 23.8 KB | Display | |
Data in CIF | ![]() | 32.9 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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Components
#1: Protein | Mass: 33444.406 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9HAN9, nicotinamide-nucleotide adenylyltransferase #2: Chemical | Sequence details | N-TERMINUS INCLUDES A HIS-TAG | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.56 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 2.0 M NA/KH2PO4, 100 M M TRIS PH 7.5, 5% 2-PROPANOL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: Werner, E., (2002) Acta Crystallogr., D58, 140. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Jun 17, 2001 / Details: MIRRORS |
Radiation | Monochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→20 Å / Num. obs: 62691 / % possible obs: 98.3 % / Observed criterion σ(I): 0.5 / Redundancy: 10.1 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.2 |
Reflection shell | Resolution: 2.9→3 Å / Rmerge(I) obs: 0.492 / Mean I/σ(I) obs: 1.1 / % possible all: 92.5 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 632186 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS % possible obs: 92.5 % / Num. unique obs: 5937 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→20 Å
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Refine LS restraints |
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