+Open data
-Basic information
Entry | Database: PDB / ID: 1ll4 | |||||||||
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Title | STRUCTURE OF C. IMMITIS CHITINASE 1 COMPLEXED WITH ALLOSAMIDIN | |||||||||
Components | CHITINASE 1 | |||||||||
Keywords | HYDROLASE / BETA-ALPHA BARREL / ENZYME-INHIBITOR COMPLEX | |||||||||
Function / homology | Function and homology information chitinase / chitinase activity / chitin catabolic process / chitin binding / polysaccharide catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | Coccidioides immitis (fungus) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | |||||||||
Authors | Bortone, K. / Monzingo, A.F. / Ernst, S. / Robertus, J.D. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: THE STRUCTURE OF AN ALLOSAMIDIN COMPLEX WITH THE Coccidioides IMMITIS CHITINASE DEFINES A ROLE FOR A SECOND ACID RESIDUE IN SUBSTRATE-ASSISTED MECHANISM Authors: BORTONE, K. / MONZINGO, A.F. / ERNST, S. / ROBERTUS, J.D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ll4.cif.gz | 312.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ll4.ent.gz | 252.8 KB | Display | PDB format |
PDBx/mmJSON format | 1ll4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ll4_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 1ll4_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 1ll4_validation.xml.gz | 60.7 KB | Display | |
Data in CIF | 1ll4_validation.cif.gz | 80.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ll/1ll4 ftp://data.pdbj.org/pub/pdb/validation_reports/ll/1ll4 | HTTPS FTP |
-Related structure data
Related structure data | 1ll6C 1ll7C 1d2kS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 43714.812 Da / Num. of mol.: 4 / Fragment: RESIDUES 36-427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Coccidioides immitis (fungus) / Gene: CTS1 / Plasmid: pGEX-4T-3 / Production host: Escherichia coli (E. coli) / References: PIR: JC4565, UniProt: P0CB51*PLUS, chitinase #2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-AMI / #4: Water | ChemComp-HOH / | |
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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: 2.18 Å3/Da / Density % sol: 43.6 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 4000, ISOPROPANOL, SODIUM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 4.6 / Method: vapor diffusion, sitting dropDetails: Hollis, T., (1998) Acta Crystallogr., Sect.D, 54, 1412. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Aug 19, 2000 |
Radiation | Monochromator: DOUBLE FOCUSSING MIRRORS (NI & PT) + NI FILTER Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. all: 34859 / Num. obs: 34859 / % possible obs: 95.8 % / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rmerge(I) obs: 0.131 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.369 / Mean I/σ(I) obs: 2.3 / Num. unique all: 3428 / % possible all: 93.2 |
Reflection | *PLUS Rmerge(I) obs: 0.131 |
Reflection shell | *PLUS Rmerge(I) obs: 0.369 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ID 1D2K Resolution: 2.8→5 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→5 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree: 0.258 / Rfactor Rwork: 0.197 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |