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Open data
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Basic information
Entry | Database: PDB / ID: 1d2k | ||||||
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Title | C. IMMITIS CHITINASE 1 AT 2.2 ANGSTROMS RESOLUTION | ||||||
![]() | CHITINASE 1 | ||||||
![]() | HYDROLASE / BETA-ALPHA BARREL | ||||||
Function / homology | ![]() chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Hollis, T. / Monzingo, A.F. / Bortone, K. / Ernst, S.R. / Cox, R. / Robertus, J.D. | ||||||
![]() | ![]() Title: The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis. Authors: Hollis, T. / Monzingo, A.F. / Bortone, K. / Ernst, S. / Cox, R. / Robertus, J.D. #1: ![]() Title: Crystallization and Preliminary X-ray Analysis of a Chitinase from the Fungal Pathogen Coccidioides immitis Authors: Hollis, T. / Monzingo, A.F. / Bortone, K. / Schelp, E. / Cox, R. / Robertus, J.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.9 KB | Display | ![]() |
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PDB format | ![]() | 69.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422.6 KB | Display | ![]() |
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Full document | ![]() | 427.5 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 26.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 43714.812 Da / Num. of mol.: 1 / Fragment: RESIDUES 36-427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P54196, UniProt: P0CB51*PLUS, chitinase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.82 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: PEG 4000, SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 25K | |||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 16, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. all: 20962 / Num. obs: 20899 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6 % / Biso Wilson estimate: 18.6 Å2 / Rmerge(I) obs: 0.122 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.213 / % possible all: 99.4 |
Reflection shell | *PLUS % possible obs: 99.4 % |
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Processing
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Refinement | Resolution: 2.2→5 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2.2→5 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.258 / Rfactor Rwork: 0.176 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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