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Open data
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Basic information
Entry | Database: PDB / ID: 1hxp | ||||||
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Title | NUCLEOTIDE TRANSFERASE | ||||||
![]() | HEXOSE-1-PHOSPHATE URIDYLYLTRANSFERASE | ||||||
![]() | NUCLEOTIDYL TRANSFERASE / METALLOENZYME / GALACTOSEMIA / COMPLEX (SERINE PROTEASE-INHIBITOR) | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Wedekind, J.E. / Frey, P.A. / Rayment, I. | ||||||
![]() | ![]() Title: Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Authors: Wedekind, J.E. / Frey, P.A. / Rayment, I. #1: ![]() Title: Galactose-1-Phosphate Uridylyltransferase from Escherichia Coli, a Zinc and Iron Metalloenzyme Authors: Ruzicka, F.J. / Wedekind, J.E. / Kim, J. / Rayment, I. / Frey, P.A. #2: ![]() Title: Crystallization and Preliminary Crystallographic Analysis of Galactose-1-Phosphate Uridylyltransferase from Escherichia Coli Authors: Wedekind, J.E. / Frey, P.A. / Rayment, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 154.4 KB | Display | ![]() |
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PDB format | ![]() | 126.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.94411, -0.01072, 0.32945), Vector: Details | THE CRYSTALLOGRAPHICALLY INDEPENDENT UNIT IS ONE DIMER OF CHEMICALLY IDENTICAL SUBUNITS. | |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 39695.582 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE-UMP/UDP COMPLEX Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 6 types, 479 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/U5P.gif)
![](data/chem/img/UDP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FE.gif)
![](data/chem/img/BME.gif)
![](data/chem/img/U5P.gif)
![](data/chem/img/UDP.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-BME / #5: Chemical | ChemComp-U5P / | #6: Chemical | ChemComp-UDP / | #7: Water | ChemComp-HOH / | |
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-Details
Compound details | THIS ENTRY REPRESENTS THE STRUCTURE OF GALACTOSE-1-PHOSPHATE URIDYLYLTRANSFERASE COMPLEXED WITH UMP ...THIS ENTRY REPRESENTS |
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Nonpolymer details | THE NUCLEOTIDE BINDS PERPENDICULARLY TO STRANDS B(ETA)-3, B(ETA)-6, B(ETA)-7 AND B(ETA)-8 OF THE ...THE NUCLEOTIDE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.89 Å3/Da / Density % sol: 57 % / Description: NUMBER OF OBSERVED REFLECTIONS = 169713 | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 277 K / pH: 5.9 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Date: 1993 |
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Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Redundancy: 2 % / Biso Wilson estimate: 24.3 Å2 / Rmerge(I) obs: 0.053 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 68553 / % possible obs: 82 % / Num. measured all: 169713 / Rmerge(I) obs: 0.022 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.94 Å / % possible obs: 70 % / Num. unique obs: 11827 / Num. measured obs: 31548 / Rmerge(I) obs: 0.096 |
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Processing
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Refinement | Resolution: 1.8→50 Å / σ(F): 0 Details: DESPITE THE PRESENCE OF THE NUCLEOTIDE PHOSPHATE(S) THE LOOP REGION ADJACENT TO THE ACTIVE SITE FROM GLY 159 THROUGH ASN 162 EXHIBITS UNUSUALLY HIGH TEMPERATURE FACTORS.
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Refinement step | Cycle: LAST / Resolution: 1.8→50 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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