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- PDB-6hki: Crystal structure of surface entropy mutant of human O-GlcNAc hyd... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6hki | ||||||
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Title | Crystal structure of surface entropy mutant of human O-GlcNAc hydrolase | ||||||
![]() | Protein O-GlcNAcase | ||||||
![]() | HYDROLASE / O-GlcNAc / deglycosylation / glycosidase | ||||||
Function / homology | ![]() hyalurononglucosaminidase activity / glycoprotein metabolic process / N-acetylglucosamine metabolic process / glycoprotein catabolic process / protein O-GlcNAcase / : / : / [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity / protein O-linked glycosylation / protein deglycosylation ...hyalurononglucosaminidase activity / glycoprotein metabolic process / N-acetylglucosamine metabolic process / glycoprotein catabolic process / protein O-GlcNAcase / : / : / [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity / protein O-linked glycosylation / protein deglycosylation / beta-N-acetylglucosaminidase activity / identical protein binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Males, A. / Davies, G.J. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural studies of a surface-entropy reduction mutant of O-GlcNAcase. Authors: Males, A. / Davies, G.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 221 KB | Display | ![]() |
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PDB format | ![]() | 168.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 447.9 KB | Display | ![]() |
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Full document | ![]() | 470.4 KB | Display | |
Data in XML | ![]() | 34.8 KB | Display | |
Data in CIF | ![]() | 47.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5m7rS S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 102904.828 Da / Num. of mol.: 2 / Mutation: E602A, E605A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.92 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.2 M sodium citrate tribasic, 17% polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 27, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9282 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→192.4 Å / Num. obs: 31103 / % possible obs: 99.8 % / Redundancy: 16.8 % / Biso Wilson estimate: 58.53 Å2 / CC1/2: 0.99 / Rpim(I) all: 0.11 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 3.3→3.3 Å / Redundancy: 17.1 % / Mean I/σ(I) obs: 1.8 / Num. unique obs: 4440 / CC1/2: 0.67 / Rpim(I) all: 0.62 / % possible all: 98.6 |
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Processing
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Refinement | Starting model: 5M7R Resolution: 3.3→192.4 Å / Cor.coef. Fo:Fc: 0.915 / Cor.coef. Fo:Fc free: 0.903 / SU B: 21.085 / SU ML: 0.324 / Cross valid method: THROUGHOUT / ESU R Free: 0.404 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 71.607 Å2
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Refinement step | Cycle: 1 / Resolution: 3.3→192.4 Å
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Refine LS restraints |
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