+Open data
-Basic information
Entry | Database: PDB / ID: 1uyt | ||||||
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Title | Acetyl-CoA carboxylase carboxyltransferase domain | ||||||
Components | ACETYL-COA CARBOXYLASE | ||||||
Keywords | TRANSFERASE / CARBOXYLASE / CARBOXYLTRANSFERASE | ||||||
Function / homology | Function and homology information Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine shuttle / carboxyl- or carbamoyltransferase activity / acetyl-CoA carboxylase / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity / malonyl-CoA biosynthetic process ...Biotin transport and metabolism / Fatty acyl-CoA biosynthesis / Carnitine shuttle / carboxyl- or carbamoyltransferase activity / acetyl-CoA carboxylase / acetyl-CoA binding / biotin carboxylase / acetyl-CoA carboxylase complex / biotin carboxylase activity / malonyl-CoA biosynthetic process / acetyl-CoA biosynthetic process / acetyl-CoA carboxylase activity / long-chain fatty acid biosynthetic process / fatty acid biosynthetic process / protein import into nucleus / endoplasmic reticulum membrane / protein homodimerization activity / mitochondrion / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.5 Å | ||||||
Authors | Zhang, H. / Tweel, B. / Tong, L. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Molecular Basis for the Inhibition of the Carboxyltransferase Domain of Acetyl-Coenzyme-A Carboxylase by Haloxyfop and Diclofop. Authors: Zhang, H. / Tweel, B. / Tong, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uyt.cif.gz | 402.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uyt.ent.gz | 329.5 KB | Display | PDB format |
PDBx/mmJSON format | 1uyt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1uyt_validation.pdf.gz | 460 KB | Display | wwPDB validaton report |
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Full document | 1uyt_full_validation.pdf.gz | 522.1 KB | Display | |
Data in XML | 1uyt_validation.xml.gz | 75.6 KB | Display | |
Data in CIF | 1uyt_validation.cif.gz | 102.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uy/1uyt ftp://data.pdbj.org/pub/pdb/validation_reports/uy/1uyt | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 83444.531 Da / Num. of mol.: 3 / Fragment: CARBOXYLTRANSFERASE, RESIDUES 1482-2218 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q00955, acetyl-CoA carboxylase #2: Water | ChemComp-HOH / | |
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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: 4.48 Å3/Da / Density % sol: 72.54 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 / Details: pH 5.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.5 / 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: NSLS / Beamline: X4A / Wavelength: 0.97898 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97898 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 130501 / % possible obs: 94 % / Redundancy: 3.5 % / Biso Wilson estimate: 36.1 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3 % / Rmerge(I) obs: 0.314 / Mean I/σ(I) obs: 4 / % possible all: 86 |
Reflection | *PLUS Highest resolution: 2.5 Å / Num. measured all: 420147 / Rmerge(I) obs: 0.069 |
Reflection shell | *PLUS Rmerge(I) obs: 0.314 |
-Processing
Software | Name: CNS / Version: 1.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER / Resolution: 2.5→27.62 Å / Rfactor Rfree error: 0.002 / Cross valid method: THROUGHOUT / σ(F): 1
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Displacement parameters | Biso mean: 51.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→27.62 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.59 Å / Rfactor Rfree error: 0.009 / Total num. of bins used: 10
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Refinement | *PLUS Lowest resolution: 27 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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