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Yorodumi- PDB-1asd: THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE REC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1asd | ||||||
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Title | THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH N-MEPLP | ||||||
Components | ASPARTATE AMINOTRANSFERASE | ||||||
Keywords | AMINOTRANSFERASE | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process / L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine-2-oxoglutarate transaminase activity / aspartate catabolic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / protein homodimerization activity / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Schumacher, C. / Ringe, D. | ||||||
Citation | Journal: To be Published Title: The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with N-Meplp Authors: Schumacher, C. / Ringe, D. #1: Journal: Biochemistry / Year: 1991 Title: Activity and Structure of the Active Site Mutants R386Y and R386F of Escherichia Coli Aspartate Aminotransferase Authors: Danishefsky, A.T. / Onnufer, J.J. / Petsko, G.A. / Ringe, D. #2: Journal: Biochemistry / Year: 1989 Title: 2.8 Angstroms Resolution Crystal Structure of an Active Site Mutant of Aspartate Aminotransferase from Escherichia Coli Authors: Smith, D.L. / Almo, S.C. / Toney, M.D. / Ringe, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1asd.cif.gz | 93 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1asd.ent.gz | 69.7 KB | Display | PDB format |
PDBx/mmJSON format | 1asd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1asd_validation.pdf.gz | 456 KB | Display | wwPDB validaton report |
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Full document | 1asd_full_validation.pdf.gz | 465.8 KB | Display | |
Data in XML | 1asd_validation.xml.gz | 10.6 KB | Display | |
Data in CIF | 1asd_validation.cif.gz | 16.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/1asd ftp://data.pdbj.org/pub/pdb/validation_reports/as/1asd | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 140 / 2: CIS PROLINE - PRO 196 | ||||||||
Details | THE MOLECULE IS A DIMER. TO GENERATE THE OTHER CHAIN ONE MUST APPLY THE CRYSTALLOGRAPHIC SYMMETRY OPERATION (X, Y, 156.4-Z) TO THE COORDINATES IN THIS ENTRY. |
-Components
#1: Protein | Mass: 43619.215 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P00509, aspartate transaminase |
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#2: Chemical | ChemComp-MPL / |
#3: Chemical | ChemComp-MAE / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | HET GROUP MPL 258 IS BOUND TO LYS 258 FORMING A PROTONATED SCHIFF BASE LINKAGE (BETWEEN NZ LYS 258 ...HET GROUP MPL 258 IS BOUND TO LYS 258 FORMING A PROTONATED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.45 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.198 / Rfactor obs: 0.198 / Highest resolution: 2.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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Refine LS restraints |
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