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Yorodumi- PDB-1bia: THE E. COLI BIOTIN HOLOENZYME SYNTHETASE(SLASH)BIO REPRESSOR CRYS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bia | ||||||
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Title | THE E. COLI BIOTIN HOLOENZYME SYNTHETASE(SLASH)BIO REPRESSOR CRYSTAL STRUCTURE DELINEATES THE BIOTIN AND DNA-BINDING DOMAINS | ||||||
Components | BirA BIFUNCTIONAL PROTEIN | ||||||
Keywords | TRANSCRIPTION REGULATION | ||||||
Function / homology | Function and homology information biotin metabolic process / biotin-[biotin carboxyl-carrier protein] ligase / biotin-[acetyl-CoA-carboxylase] ligase activity / biotin biosynthetic process / biotin binding / transcription repressor complex / protein modification process / nucleic acid binding / transcription cis-regulatory region binding / regulation of DNA-templated transcription ...biotin metabolic process / biotin-[biotin carboxyl-carrier protein] ligase / biotin-[acetyl-CoA-carboxylase] ligase activity / biotin biosynthetic process / biotin binding / transcription repressor complex / protein modification process / nucleic acid binding / transcription cis-regulatory region binding / regulation of DNA-templated transcription / protein homodimerization activity / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Wilson, K.P. / Shewchuk, L.M. / Matthews, B.W. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1992 Title: Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Authors: Wilson, K.P. / Shewchuk, L.M. / Brennan, R.G. / Otsuka, A.J. / Matthews, B.W. #1: Journal: J.Biol.Chem. / Year: 1989 Title: Crystallization of the Bifunctional Biotin Operon Repressor Authors: Brennan, R.G. / Vasu, S. / Matthews, B.W. / Otsuka, A.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bia.cif.gz | 67.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bia.ent.gz | 50.1 KB | Display | PDB format |
PDBx/mmJSON format | 1bia.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bi/1bia ftp://data.pdbj.org/pub/pdb/validation_reports/bi/1bia | HTTPS FTP |
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-Related structure data
-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 174 |
-Components
#1: Protein | Mass: 35351.918 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) References: UniProt: P06709, biotin-[biotin carboxyl-carrier protein] ligase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.52 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 20 Å / % possible obs: 70 % / Rmerge(I) obs: 0.075 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.19 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 20 Å / Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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