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Yorodumi- PDB-1ctn: CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ctn | ||||||
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Title | CRYSTAL STRUCTURE OF A BACTERIAL CHITINASE AT 2.3 ANGSTROMS RESOLUTION | ||||||
Components | CHITINASE AChitinase A N-terminal domain | ||||||
Keywords | LYASE (OXO-ACID) | ||||||
Function / homology | Function and homology information chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process Similarity search - Function | ||||||
Biological species | Serratia marcescens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Perrakis, A. / Tews, I. / Dauter, Z. / Wilson, K.S. / Vorgias, C.E. | ||||||
Citation | Journal: Structure / Year: 1994 Title: Crystal structure of a bacterial chitinase at 2.3 A resolution. Authors: Perrakis, A. / Tews, I. / Dauter, Z. / Oppenheim, A.B. / Chet, I. / Wilson, K.S. / Vorgias, C.E. #1: Journal: CHITIN ENZYMOL. / Year: 1993 Title: Purification and Characterization of the Recombinant Chtin Degrading Enzymes Chitinase a and Chitobiase from Serratia Marcescens Authors: Vorgias, C.E. / Tews, I. / Perrakis, A. / Oppenheim, A.B. / Wilson, K.S. #2: Journal: Embo J. / Year: 1986 Title: Isolation and Characterization of Genes Encoding Two Chitinase Enzymes from Serratia Marcescens Authors: Jones, J.D.G. / Grady, K.L. / Suslow, T.V. / Bedbrook, J.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ctn.cif.gz | 119.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ctn.ent.gz | 95.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ctn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ct/1ctn ftp://data.pdbj.org/pub/pdb/validation_reports/ct/1ctn | HTTPS FTP |
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-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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Atom site foot note | 1: CIS PEPTIDE: GLY 190 - PHE 191 / 2: CIS PEPTIDE: GLU 315 - PHE 316 / 3: CIS PEPTIDE: TRP 539 - GLU 54 |
-Components
#1: Protein | Mass: 58669.613 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Serratia marcescens (bacteria) / Plasmid: PBR322 DERIVATIVE GENE: / References: UniProt: P07254, chitinase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.47 Å3/Da / Density % sol: 64.55 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: microdialysis / Details: Vorgias, C. E., (1992) J. Mol. Bio., 226, 897. | ||||||||||||||||||||||||
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: 38115 / % possible obs: 97.2 % / Observed criterion σ(I): 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Observed criterion σ(I): 12.5 / Redundancy: 5.2 % / Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS Rmerge(I) obs: 0.246 / Mean I/σ(I) obs: 5.1 |
-Processing
Software |
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Refinement | Resolution: 2.3→10 Å / σ(F): 1 /
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Displacement parameters | Biso mean: 25.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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Refinement | *PLUS σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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