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Open data
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Basic information
Entry | Database: PDB / ID: 1ll6 | ||||||
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Title | STRUCTURE OF THE D169N MUTANT OF C. IMMITIS CHITINASE 1 | ||||||
![]() | 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 | ![]() ![]() | ||||||
![]() | Bortone, K. / Monzingo, A.F. / Ernst, S. / Robertus, J.D. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 304.6 KB | Display | ![]() |
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PDB format | ![]() | 246.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.1 KB | Display | ![]() |
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Full document | ![]() | 472.6 KB | Display | |
Data in XML | ![]() | 35.2 KB | Display | |
Data in CIF | ![]() | 52.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ll4SC ![]() 1ll7C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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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: 43713.824 Da / Num. of mol.: 4 / Fragment: RESIDUES 36-427 / Mutation: D169N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P54196, UniProt: P0CB51*PLUS, chitinase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.52 % |
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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 |
-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 3, 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: 34083 / Num. obs: 34083 / % possible obs: 94 % / Observed criterion σ(I): 0 / Redundancy: 1.7 % / Rmerge(I) obs: 0.106 / Net I/σ(I): 6.2 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.221 / Mean I/σ(I) obs: 2.4 / Num. unique all: 3261 / % possible all: 89.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ID 1LL4 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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