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- PDB-1hot: GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE ALLOSTERIC A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hot | ||||||
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Title | GLUCOSAMINE 6-PHOSPHATE DEAMINASE COMPLEXED WITH THE ALLOSTERIC ACTIVATOR N-ACETYL-GLUCOSAMINE-6-PHOSPHATE | ||||||
![]() | GLUCOSAMINE 6-PHOSPHATE DEAMINASE | ||||||
![]() | ISOMERASE | ||||||
Function / homology | ![]() glucosamine catabolic process / glucosamine-6-phosphate deaminase / glucosamine-6-phosphate deaminase activity / N-acetylglucosamine catabolic process / N-acetylglucosamine metabolic process / N-acetylneuraminate catabolic process / UDP-N-acetylglucosamine biosynthetic process / carbohydrate metabolic process / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Oliva, G. / Fontes, M.L. / Garratt, R. / Altamirano, M.M. / Calcagno, M.L. / Horjales, E. | ||||||
![]() | ![]() Title: Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Authors: Oliva, G. / Fontes, M.R. / Garratt, R.C. / Altamirano, M.M. / Calcagno, M.L. / Horjales, E. #1: ![]() Title: Crystallization and Preliminary Crystallographic Studies of Glucosamine-6-Phosphate Deaminase from Escherichia Coli K12 Authors: Horjales, E. / Altamirano, M.M. / Calcagno, M.L. / Dauter, Z. / Wilson, K. / Garratt, R.C. / Oliva, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 117 KB | Display | ![]() |
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PDB format | ![]() | 92.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 498.7 KB | Display | ![]() |
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Full document | ![]() | 507.8 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 19.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29812.211 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P09375, UniProt: P0A759*PLUS, EC: 5.3.1.10 #2: Sugar | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.7 % | |||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8.2 / 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 | *PLUS Num. obs: 20036 / % possible obs: 88.1 % / Redundancy: 1.7 % / Rmerge(I) obs: 0.051 |
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Processing
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Refinement | Resolution: 2.4→8 Å / Rfactor Rwork: 0.165 / Rfactor obs: 0.165 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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