+Open data
-Basic information
Entry | Database: PDB / ID: 1gup | ||||||
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Title | STRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GALACTOSE | ||||||
Components | GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE | ||||||
Keywords | NUCLEOTIDYLTRANSFERASE / TRANSFERASE / GALACTOSE METABOLISM | ||||||
Function / homology | Function and homology information UDP-glucose-hexose-1-phosphate uridylyltransferase / UDP-glucose:hexose-1-phosphate uridylyltransferase activity / galactokinase activity / galactose catabolic process via UDP-galactose / ferrous iron binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Thoden, J.B. / Rayment, I. / Holden, H. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site. Authors: Thoden, J.B. / Ruzicka, F.J. / Frey, P.A. / Rayment, I. / Holden, H.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gup.cif.gz | 321.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gup.ent.gz | 256.5 KB | Display | PDB format |
PDBx/mmJSON format | 1gup.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gup_validation.pdf.gz | 658.2 KB | Display | wwPDB validaton report |
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Full document | 1gup_full_validation.pdf.gz | 727.8 KB | Display | |
Data in XML | 1gup_validation.xml.gz | 38.2 KB | Display | |
Data in CIF | 1gup_validation.cif.gz | 60.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gu/1gup ftp://data.pdbj.org/pub/pdb/validation_reports/gu/1gup | 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
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 39613.500 Da / Num. of mol.: 4 / Mutation: H166G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P09148, EC: 2.7.7.10 |
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-Non-polymers , 5 types, 1265 molecules
#2: Chemical | ChemComp-GDU / #3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-FE / #5: Chemical | ChemComp-K / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.04 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Detector | Type: BRUKER NONIUS HI-STAR / Detector: MULTIWIRE AREA DETECTOR / Details: SUPER LONG DOUBLE-FOCUSING MIRRORS |
Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 123193 / % possible obs: 90 % |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 30 Å / Num. measured all: 244754 / Rmerge(I) obs: 0.047 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / % possible obs: 83 % / Num. unique obs: 13689 / Num. measured obs: 20254 / Rmerge(I) obs: 0.099 |
-Processing
Software |
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Refinement | Resolution: 1.8→30 Å /
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.191 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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