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Yorodumi- PDB-1spa: ROLE OF ASP222 IN THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1spa | ||||||
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Title | ROLE OF ASP222 IN THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE: THE AMINO ACID RESIDUE WHICH ENHANCES THE FUNCTION OF THE ENZYME-BOUND COENZYME PYRIDOXAL 5'-PHOSPHATE | ||||||
Components | ASPARTATE AMINOTRANSFERASE | ||||||
Keywords | TRANSFERASE(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 Å | ||||||
Authors | Hinoue, Y. / Yano, T. / Metzler, D.E. / Miyahara, I. / Hirotsu, K. / Kagamiyama, H. | ||||||
Citation | Journal: Biochemistry / Year: 1992 Title: Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate. Authors: Yano, T. / Kuramitsu, S. / Tanase, S. / Morino, Y. / Kagamiyama, H. #1: Journal: To be Published Title: Role of an Active Site Residue Analyzed by Combination of Mutagenesis and Coenzyme Analogue Authors: Yano, T. / Hinoue, Y. / Chen, V.J. / Metzler, D.E. / Miyahara, I. / Hirotsu, K. / Kagamiyama, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1spa.cif.gz | 91 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1spa.ent.gz | 68.6 KB | Display | PDB format |
PDBx/mmJSON format | 1spa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1spa_validation.pdf.gz | 451.3 KB | Display | wwPDB validaton report |
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Full document | 1spa_full_validation.pdf.gz | 469 KB | Display | |
Data in XML | 1spa_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 1spa_validation.cif.gz | 17.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sp/1spa ftp://data.pdbj.org/pub/pdb/validation_reports/sp/1spa | 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 138 / 2: CIS PROLINE - PRO 195 |
-Components
#1: Protein | Mass: 43575.203 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-NPL / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.36 % |
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-Processing
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Refinement | Rfactor Rwork: 0.209 / Rfactor obs: 0.209 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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