+Open data
-Basic information
Entry | Database: PDB / ID: 1hgw | ||||||
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Title | CEL6A D175A mutant | ||||||
Components | CELLOBIOHYDROLASE CEL6A (FORMERLY CALLED CBH II) | ||||||
Keywords | HYDROLASE (O-GLYCOSYL) / GLYCOSIDASE / GLYCOPROTEIN | ||||||
Function / homology | Function and homology information cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | TRICHODERMA REESEI (fungus) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Zou, J.-Y. / Jones, T.A. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2002 Title: The Active Site of Cellobiohydrolase Cel6A from Trichoderma Reesei: The Roles of Aspartic Acids D221 and D175 Authors: Koivula, A. / Ruohonen, L. / Wohlfahrt, G. / Reinikainen, T. / Teeri, T.T. / Piens, K. / Claeyssens, M. / Weber, M. / Vasella, A. / Becker, D. / Sinnott, M.L. / Zou, J.-Y. / Kleywegt, G.J. / ...Authors: Koivula, A. / Ruohonen, L. / Wohlfahrt, G. / Reinikainen, T. / Teeri, T.T. / Piens, K. / Claeyssens, M. / Weber, M. / Vasella, A. / Becker, D. / Sinnott, M.L. / Zou, J.-Y. / Kleywegt, G.J. / Szardenings, M. / Stahlberg, J. / Jones, T.A. #1: Journal: Science / Year: 1990 Title: Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma Reesei Authors: Rouvinen, J. / Bergfors, T. / Teeri, T. / Knowles, J.K. / Jones, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hgw.cif.gz | 160.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hgw.ent.gz | 126.8 KB | Display | PDB format |
PDBx/mmJSON format | 1hgw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1hgw_validation.pdf.gz | 486.1 KB | Display | wwPDB validaton report |
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Full document | 1hgw_full_validation.pdf.gz | 493.3 KB | Display | |
Data in XML | 1hgw_validation.xml.gz | 32.2 KB | Display | |
Data in CIF | 1hgw_validation.cif.gz | 47.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hg/1hgw ftp://data.pdbj.org/pub/pdb/validation_reports/hg/1hgw | HTTPS FTP |
-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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.999999, -0.001278, -0.000251), Vector: |
-Components
#1: Protein | Mass: 39011.285 Da / Num. of mol.: 2 / Fragment: CATALYTIC DOMAIN, RESIDUES 83-447 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) TRICHODERMA REESEI (fungus) / Gene: CBH2 (D175A) / Gene (production host): CBH2 (D175A) / Production host: TRICHODERMA REESEI (fungus) References: UniProt: P07987, cellulose 1,4-beta-cellobiosidase (non-reducing end) #2: Sugar | ChemComp-NAG / #3: Sugar | ChemComp-MAN / #4: Chemical | ChemComp-CO / | #5: Water | ChemComp-HOH / | Compound details | CHAIN A, B ENGINEERED MUTATION ASP 175 ALA. HYDROLYSIS OF 1,4-BETA-D-GLUCOSIDIC LINKAGES IN ...CHAIN A, B ENGINEERED | |
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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: 2.07 Å3/Da / Density % sol: 40.56 % | ||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: 20% PEG6000, 20MM MES BUFFER PH 10MM COCL2. | ||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Bergfors, T., (1989) J.Mol.Biol, 209, 167. | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: MSC / Detector: IMAGE PLATE / Date: Apr 29, 1996 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→47.1 Å / Num. obs: 37025 / % possible obs: 99.5 % / Redundancy: 2.8 % / Biso Wilson estimate: 10.5 Å2 / Rmerge(I) obs: 0.049 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.118 / Mean I/σ(I) obs: 7.8 / % possible all: 99.9 |
Reflection | *PLUS Lowest resolution: 80 Å |
Reflection shell | *PLUS % possible obs: 99.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: WILDTYPE CEL6A Resolution: 2.1→19.97 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 1649550.7 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: BULK SOLVENT MODEL USED THE CATALYTIC CORE STARTS AT RESIDUE 83.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 46 Å2 / ksol: 0.38051 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.1→19.97 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.23 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.183 |