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Yorodumi- PDB-2b3v: Spermine spermidine acetyltransferase in complex with acetylcoa, ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2b3v | ||||||
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Title | Spermine spermidine acetyltransferase in complex with acetylcoa, K26R mutant | ||||||
Components | Diamine acetyltransferase 1 | ||||||
Keywords | TRANSFERASE / polyamine / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC | ||||||
Function / homology | Function and homology information Interconversion of polyamines / spermidine acetylation / spermidine binding / putrescine catabolic process / polyamine biosynthetic process / diamine N-acetyltransferase / diamine N-acetyltransferase activity / N-acetyltransferase activity / angiogenesis / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.95 Å | ||||||
Authors | Bewley, M.C. / Graziano, V. / Jiang, J.S. / Matz, E. / Studier, F.W. / Pegg, A.P. / Coleman, C.S. / Flanagan, J.M. / Burley, S.K. / New York SGX Research Center for Structural Genomics (NYSGXRC) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2006 Title: Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Authors: Bewley, M.C. / Graziano, V. / Jiang, J. / Matz, E. / Studier, F.W. / Pegg, A.E. / Coleman, C.S. / Flanagan, J.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2b3v.cif.gz | 45.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2b3v.ent.gz | 35.8 KB | Display | PDB format |
PDBx/mmJSON format | 2b3v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b3/2b3v ftp://data.pdbj.org/pub/pdb/validation_reports/b3/2b3v | HTTPS FTP |
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-Related structure data
Related structure data | 2b3uC 2b4bC 2b4dC 2b58C 2b5gC 2b47 C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20404.268 Da / Num. of mol.: 1 / Mutation: K26R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SAT / Plasmid: pET13a / Production host: Escherichia coli (E. coli) / References: UniProt: P21673, diamine N-acetyltransferase |
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#2: Chemical | ChemComp-ACO / |
#3: 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: 2.27 Å3/Da / Density % sol: 45.83 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: mmPEG5000, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 0.98 Å |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→30 Å / Num. obs: 12884 / % possible obs: 96.6 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.95→30 Å / σ(F): -3 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.95→30 Å
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