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Yorodumi- PDB-1png: CRYSTAL STRUCTURE OF PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ... -
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-Basic information
Entry | Database: PDB / ID: 1png | ||||||
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Title | CRYSTAL STRUCTURE OF PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ASPARAGINE AMIDASE AT 2.2 ANGSTROMS RESOLUTION | ||||||
Components | PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL)ASPARAGINE AMIDASE F | ||||||
Keywords | HYDROLASE | ||||||
Function / homology | Function and homology information oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen / peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase / peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity Similarity search - Function | ||||||
Biological species | Elizabethkingia meningoseptica (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Van Roey, P. / Kuhn, P. | ||||||
Citation | Journal: Biochemistry / Year: 1994 Title: Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution. Authors: Kuhn, P. / Tarentino, A.L. / Plummer Jr., T.H. / Van Roey, P. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystallization and Preliminary Crystallographic Analysis of Peptide-N(4)-(N-Acetyl-Beta-D-Glucosaminyl) Asparagine Amidase (Pngasef) Authors: Kuhn, P. / Tarentino, A.L. / Plummer Junior, T.H. / Van Roey, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
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PDBx/mmCIF format | 1png.cif.gz | 72.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1png.ent.gz | 57.6 KB | Display | PDB format |
PDBx/mmJSON format | 1png.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pn/1png ftp://data.pdbj.org/pub/pdb/validation_reports/pn/1png | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 196 / 2: CIS PROLINE - PRO 241 / 3: RESIDUES CYS 204 - ALA 205 FORM A CIS PEPTIDE. |
-Components
#1: Protein | Mass: 34815.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Elizabethkingia meningoseptica (bacteria) References: UniProt: P21163, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 60.37 % | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 10 ℃ / pH: 4.3 / 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 Highest resolution: 2.2 Å / Num. obs: 22074 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Num. measured all: 95693 / Rmerge F obs: 0.056 |
-Processing
Refinement | Resolution: 2.2→49.1 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.2→49.1 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rwork: 0.183 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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