+Open data
-Basic information
Entry | Database: PDB / ID: 2eng | |||||||||
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Title | ENDOGLUCANASE V | |||||||||
Components | ENDOGLUCANASE V | |||||||||
Keywords | HYDROLASE (ENDOGLUCANASE) / CELLULOSE DEGRADATION / GLYCOSIDASE | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Humicola insolens (fungus) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.5 Å | |||||||||
Authors | Davies, G.J. / Schulein, M. | |||||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution. Authors: Davies, G.J. / Tolley, S.P. / Henrissat, B. / Hjort, C. / Schulein, M. #1: Journal: Nature / Year: 1993 Title: Structure and Function of Endoglucanase V Authors: Davies, G.J. / Dodson, G.G. / Hubbard, R.E. / Tolley, S.P. / Dauter, Z. / Wilson, K.S. / Hjort, C. / Mikkelsen, J.M. / Rasmussen, G. / Schulein, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eng.cif.gz | 52.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eng.ent.gz | 40.9 KB | Display | PDB format |
PDBx/mmJSON format | 2eng.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2eng_validation.pdf.gz | 389.6 KB | Display | wwPDB validaton report |
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Full document | 2eng_full_validation.pdf.gz | 390.4 KB | Display | |
Data in XML | 2eng_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 2eng_validation.cif.gz | 10 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/en/2eng ftp://data.pdbj.org/pub/pdb/validation_reports/en/2eng | HTTPS FTP |
-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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-Components
#1: Protein | Mass: 22545.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Humicola insolens (fungus) / References: UniProt: P43316, cellulase |
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#2: Water | ChemComp-HOH / |
Compound details | ENDOGLUCAN |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.01 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS 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: 1.48 Å |
-Processing
Software | Name: SHELXL / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.5→10 Å Details: THE SECOND (LESSER) CONFORMATION FOR THE SIDE CHAIN OF ASP 121 MAKES A STERIC CLASH WITH THE SIDE CHAIN OF HIS 119. HIS 119 HAS THEREFORE BEEN REFINED WITH A PARTIAL OCCUPANCY OF 0.6. THE ...Details: THE SECOND (LESSER) CONFORMATION FOR THE SIDE CHAIN OF ASP 121 MAKES A STERIC CLASH WITH THE SIDE CHAIN OF HIS 119. HIS 119 HAS THEREFORE BEEN REFINED WITH A PARTIAL OCCUPANCY OF 0.6. THE ISOTROPIC TEMPERATURE FACTORS GIVEN ARE CALCULATED BY CONVERSION FROM THE ANISOTROPIC DISPLACEMENT PARAMETERS. A COORDINATE SET WITH ANISOTROPIC DISPLACEMENT PARAMETERS WILL BE SUBMITTED SOON.
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Refinement step | Cycle: LAST / Resolution: 1.5→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELX / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.105 | ||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |