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Yorodumi- PDB-1b5s: DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RES... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1b5s | ||||||
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Title | DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS | ||||||
Components | DIHYDROLIPOAMIDE ACETYLTRANSFERASE | ||||||
Keywords | ACYLTRANSFERASE / DIHYDROLIPOYL TRANSACETYLASE / PYRUVATE DEHYDROGENASE / E2P / DIHYDROLIPOYL ACETYLTRANSFERASE | ||||||
Function / homology | Function and homology information dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / lipoic acid binding / cytoplasm Similarity search - Function | ||||||
Biological species | Geobacillus stearothermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.4 Å | ||||||
Authors | Izard, T. / Aevarsson, A. / Allen, M.D. / Westphal, A.H. / Perham, R.N. / De Kok, A. / Hol, W.G. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 Title: Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Authors: Izard, T. / Aevarsson, A. / Allen, M.D. / Westphal, A.H. / Perham, R.N. / de Kok, A. / Hol, W.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b5s.cif.gz | 165.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b5s.ent.gz | 112.5 KB | Display | PDB format |
PDBx/mmJSON format | 1b5s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b5/1b5s ftp://data.pdbj.org/pub/pdb/validation_reports/b5/1b5s | HTTPS FTP |
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-Related structure data
Related structure data | 1eaaS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 26436.783 Da / Num. of mol.: 5 / Fragment: CATALYTIC DOMAIN / Source method: isolated from a natural source / Source: (natural) Geobacillus stearothermophilus (bacteria) References: UniProt: P11961, dihydrolipoyllysine-residue acetyltransferase |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.01 Å3/Da / Density % sol: 59.1 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: May 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 4.4→50 Å / Num. obs: 34381 / % possible obs: 63.4 % / Observed criterion σ(I): 1 / Redundancy: 6.4 % / Rmerge(I) obs: 0.083 |
Reflection shell | Resolution: 4.4→4.68 Å / Rmerge(I) obs: 0.387 / % possible all: 34.9 |
Reflection | *PLUS Num. measured all: 219513 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1EAA Highest resolution: 4.4 Å / Details: NOT YET FULLY REFINED. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 4.4 Å
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