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Yorodumi- PDB-1p88: Substrate-induced structural changes to the isolated N-terminal d... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1p88 | ||||||
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Title | Substrate-induced structural changes to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase | ||||||
Components | 3-phosphoshikimate 1-carboxyvinyltransferase | ||||||
Keywords | TRANSFERASE / EPSP synthase / NMR Structure from MOLMOL | ||||||
Function / homology | Function and homology information 3-phosphoshikimate 1-carboxyvinyltransferase / 3-phosphoshikimate 1-carboxyvinyltransferase activity / chorismate biosynthetic process / aromatic amino acid family biosynthetic process / amino acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / CNS | ||||||
Model type details | minimized average | ||||||
Authors | Young, J.K. / Stauffer, M.E. / Kim, H.J. / Helms, G.L. / Evans, J.N.S. | ||||||
Citation | Journal: To be Published Title: Letter: Substrate-induced structural changes to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase Authors: Young, J.K. / Stauffer, M.E. / Kim, H.J. / Helms, G.L. / Evans, J.N.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p88.cif.gz | 704.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p88.ent.gz | 587.5 KB | Display | PDB format |
PDBx/mmJSON format | 1p88.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1p88_validation.pdf.gz | 350.8 KB | Display | wwPDB validaton report |
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Full document | 1p88_full_validation.pdf.gz | 503.8 KB | Display | |
Data in XML | 1p88_validation.xml.gz | 77.4 KB | Display | |
Data in CIF | 1p88_validation.cif.gz | 105.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p8/1p88 ftp://data.pdbj.org/pub/pdb/validation_reports/p8/1p88 | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 23139.447 Da / Num. of mol.: 1 / Fragment: n-terminal domain (25-240) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: O157 / Gene: AROA OR B0908 OR Z1254 OR ECS0991 / Production host: Escherichia coli (E. coli) References: UniProt: P0A6D3, 3-phosphoshikimate 1-carboxyvinyltransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: CNS / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 10 / Conformers submitted total number: 11 |