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Yorodumi- PDB-1xyo: STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM T... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xyo | |||||||||
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Title | STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI | |||||||||
Components | ENDO-1,4-BETA-XYLANASE IIXylanase | |||||||||
Keywords | HYDROLASE / XYLANASE | |||||||||
Function / homology | Function and homology information endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | Hypocrea jecorina (fungus) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.5 Å | |||||||||
Authors | Rouvinen, J. / Torronen, A. | |||||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei. Authors: Torronen, A. / Rouvinen, J. #1: Journal: Embo J. / Year: 1994 Title: Three-Dimensional Structure of Endo-1,4-Beta-Xylanase II from Trichoderma Reesei: Two Conformational States in the Active Site Authors: Torronen, A. / Harkki, A. / Rouvinen, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xyo.cif.gz | 84.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xyo.ent.gz | 68.8 KB | Display | PDB format |
PDBx/mmJSON format | 1xyo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xy/1xyo ftp://data.pdbj.org/pub/pdb/validation_reports/xy/1xyo | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 53 / 2: CIS PROLINE - PRO A 83 / 3: CIS PROLINE - PRO B 53 / 4: CIS PROLINE - PRO B 83 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.9866, -0.024599, 0.1616), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 1 .. A 190 B 1 .. B 190 0.245 | |
-Components
#1: Protein | Mass: 20838.436 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hypocrea jecorina (fungus) / References: UniProt: P36217, endo-1,4-beta-xylanase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.61 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.2 / Method: vapor diffusion, hanging drop / Details: Torronen, A., (1993) J. Mol. Biol., 233, 313. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jul 10, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 41141 / % possible obs: 68 % / Observed criterion σ(F): 1 / Redundancy: 1.9 % / Rmerge(I) obs: 0.0778 |
Reflection | *PLUS Highest resolution: 1.5 Å / Num. measured all: 78692 / Rmerge(I) obs: 0.0778 |
-Processing
Software |
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Refinement | Resolution: 1.5→8 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 17.81 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→8 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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