+Open data
-Basic information
Entry | Database: PDB / ID: 1nah | |||||||||
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Title | UDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLI, REDUCED | |||||||||
Components | UDP-GALACTOSE 4-EPIMERASE | |||||||||
Keywords | ISOMERASE | |||||||||
Function / homology | Function and homology information colanic acid biosynthetic process / racemase and epimerase activity, acting on carbohydrates and derivatives / UDP-glucose 4-epimerase / UDP-glucose 4-epimerase activity / galactose catabolic process via UDP-galactose / galactose metabolic process / NAD+ binding / carbohydrate metabolic process / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | |||||||||
Authors | Thoden, J.B. / Frey, P.A. / Holden, H.M. | |||||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli. Authors: Thoden, J.B. / Frey, P.A. / 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 | 1nah.cif.gz | 95 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nah.ent.gz | 69.7 KB | Display | PDB format |
PDBx/mmJSON format | 1nah.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nah_validation.pdf.gz | 540.1 KB | Display | wwPDB validaton report |
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Full document | 1nah_full_validation.pdf.gz | 548.8 KB | Display | |
Data in XML | 1nah_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 1nah_validation.cif.gz | 17.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/1nah ftp://data.pdbj.org/pub/pdb/validation_reports/na/1nah | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 37294.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: REDUCED FORM / Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PT7E2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3), PLYSS / References: UniProt: P09147, UDP-glucose 4-epimerase |
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-Non-polymers , 6 types, 498 molecules
#2: Chemical | #3: Chemical | ChemComp-NAD / | #4: Chemical | ChemComp-UDP / | #5: Chemical | ChemComp-EDO / | #6: Chemical | ChemComp-PEG / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.93 % | ||||||||||||||||||||||||||||||||||||||||||
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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
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 39891 / % possible obs: 97 % |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 30 Å / Num. measured all: 72653 / Rmerge(I) obs: 0.021 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / % possible obs: 94 % / Num. unique obs: 7216 / Num. measured obs: 10601 / Rmerge(I) obs: 0.076 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→30 Å / Details: TNT /
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Refinement step | Cycle: LAST / Resolution: 1.8→30 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.165 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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