+Open data
-Basic information
Entry | Database: PDB / ID: 2b4b | ||||||
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Title | SSAT+COA+BE-3-3-3, K26R mutant | ||||||
Components | Diamine acetyltransferase 1 | ||||||
Keywords | TRANSFERASE / 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 / SAD / Resolution: 2 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.S. / Matz, E. / Studier, F.W. / Pegg, A.P. / 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 | 2b4b.cif.gz | 82.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2b4b.ent.gz | 67.5 KB | Display | PDB format |
PDBx/mmJSON format | 2b4b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b4/2b4b ftp://data.pdbj.org/pub/pdb/validation_reports/b4/2b4b | HTTPS FTP |
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-Related structure data
Related structure data | 2b3uC 2b3vC 2b4dC 2b58C 2b5gC 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.: 2 / Mutation: K26R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SAT1, SAT / Production host: Escherichia coli (E. coli) / References: UniProt: P21673, diamine N-acetyltransferase #2: Chemical | #3: Chemical | ChemComp-B33 / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.47 % |
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-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 23363 / Num. obs: 21641 |
-Processing
Software | Name: CNS / Version: 1.1 / Classification: refinement | |||||||||||||||
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Refinement | Method to determine structure: SAD / Resolution: 2→30 Å / σ(F): -3
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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