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Yorodumi- PDB-1k5c: Endopolygalacturonase I from Stereum purpureum at 0.96 A resolution -
+Open data
-Basic information
Entry | Database: PDB / ID: 1k5c | ||||||
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Title | Endopolygalacturonase I from Stereum purpureum at 0.96 A resolution | ||||||
Components | ENDOPOLYGALACTURONASEPolygalacturonase | ||||||
Keywords | HYDROLASE / BETA HELICAL STRUCTURE / GLYCOSIDE HYDROLASE / SILVER-LEAF INDUCING SUBSTANCE | ||||||
Function / homology | Function and homology information endo-polygalacturonase / polygalacturonase activity / pectin catabolic process / cell wall organization / extracellular region Similarity search - Function | ||||||
Biological species | Chondrostereum purpureum (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 0.96 Å | ||||||
Authors | Shimizu, T. / Nakatsu, T. / Miyairi, K. / Okuno, T. / Kato, H. | ||||||
Citation | Journal: Biochemistry / Year: 2002 Title: Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution. Authors: Shimizu, T. / Nakatsu, T. / Miyairi, K. / Okuno, T. / Kato, H. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Crystallization and preliminary X-ray study of endopolygalacturonase from the pathogenic fungus Stereum purpureum Authors: Shimizu, T. / Nakatsu, T. / Miyairi, K. / Okuno, T. / Kato, H. #2: Journal: Eur.J.Biochem. / Year: 2000 Title: Determination of glycosylation sites, disulfide bridges, and the C-terminus of Stereum purpureum mature endopolygalacturonase I by electrospray ionization mass spectrometry Authors: Shimizu, T. / Miyairi, K. / Okuno, T. #3: Journal: BIOSCI.BIOTECHNOL.BIOCHEM. / Year: 1998 Title: Isolation, characterization, and sugar chain structure of endoPG Ia, Ib and Ic from Stereum purpureum Authors: Hasui, Y. / Fukui, Y. / Kikuchi, J. / Kato, N. / Miyairi, K. / Okuno, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1k5c.cif.gz | 153.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1k5c.ent.gz | 123.9 KB | Display | PDB format |
PDBx/mmJSON format | 1k5c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k5/1k5c ftp://data.pdbj.org/pub/pdb/validation_reports/k5/1k5c | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 34652.363 Da / Num. of mol.: 1 / Fragment: residues 1-335 / Source method: isolated from a natural source / Source: (natural) Chondrostereum purpureum (fungus) / Strain: ASP-4B / References: UniProt: P79074, endo-polygalacturonase | ||||||
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#2: Sugar | #3: Chemical | ChemComp-CL / | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.61 Å3/Da / Density % sol: 44.69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5 Details: PEG 4000, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 0.7 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Dec 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.7 Å / Relative weight: 1 |
Reflection | Resolution: 0.96→41.5 Å / Num. all: 171534 / Num. obs: 171534 / % possible obs: 94 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 6.9 % / Biso Wilson estimate: 11.2 Å2 / Rsym value: 0.037 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 0.96→1.01 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 3.5 / Rsym value: 0.206 / % possible all: 89.4 |
Reflection | *PLUS Num. measured all: 1186116 / Rmerge(I) obs: 0.037 |
Reflection shell | *PLUS % possible obs: 89.4 % / Rmerge(I) obs: 0.206 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 0.96→10 Å / Num. parameters: 27168 / Num. restraintsaints: 32409 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 17 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 2897.1 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.96→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / Rfactor all: 0.114 / Rfactor Rfree: 0.14 / Rfactor Rwork: 0.114 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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