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- PDB-1enx: STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM T... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1enx | |||||||||
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Title | STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI | |||||||||
![]() | ENDO-1,4-BETA-XYLANASE II | |||||||||
![]() | HYDROLASE / XYLANASE | |||||||||
Function / homology | ![]() endo-1,4-beta-xylanase activity / endo-1,4-beta-xylanase / xylan catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Rouvinen, J. / Torronen, A. | |||||||||
![]() | ![]() Title: Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei. Authors: Torronen, A. / Rouvinen, J. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.4 KB | Display | ![]() |
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PDB format | ![]() | 69.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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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: (0.9869, -0.0241, 0.1598), 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 0.232 | |
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Components
#1: Protein | Mass: 20838.436 Da / Num. of mol.: 2 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: 2.26 Å3/Da / Density % sol: 45.62 % | |||||||||||||||||||||||||
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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
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 46045 / % possible obs: 76 % / Observed criterion σ(F): 1 |
Reflection | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 8 Å / Num. measured all: 86310 / Rmerge F obs: 0.0916 |
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Processing
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Refinement | Resolution: 1.5→8 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 16.92 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→8 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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