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- PDB-2rva: Solution structure of chitosan-binding module 2 derived from chit... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2rva | ||||||
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Title | Solution structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 | ||||||
![]() | Glucanase | ||||||
![]() | HYDROLASE / carbohydrate-binding module / CBM / chitosanase | ||||||
Function / homology | ![]() Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / polysaccharide catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / na | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Shinya, S. / Nishimura, S. / Fukamizo, T. | ||||||
![]() | ![]() Title: Mechanism of chitosan recognition by CBM32 carbohydrate-binding modules from a Paenibacillus sp. IK-5 chitosanase/glucanase. Authors: Shinya, S. / Nishimura, S. / Kitaoku, Y. / Numata, T. / Kimoto, H. / Kusaoke, H. / Ohnuma, T. / Fukamizo, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 381.2 KB | Display | ![]() |
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PDB format | ![]() | 314.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 464.7 KB | Display | ![]() |
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Full document | ![]() | 663.1 KB | Display | |
Data in XML | ![]() | 46 KB | Display | |
Data in CIF | ![]() | 53.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2rv9C ![]() 4zxeC ![]() 4zy9C ![]() 4zz5C ![]() 4zz8C 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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NMR ensembles |
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Components
#1: Protein | Mass: 14910.056 Da / Num. of mol.: 1 / Fragment: chitosan-binding module 2, UNP residues 666-796 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: Paenibacillus fukuinensis has been renamed to Paenibacillus sp. IK-5. Production host: ![]() ![]() References: UniProt: Q93IE7, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample |
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Sample conditions | pH: 7.0 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: na / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 28000 / Conformers submitted total number: 10 / Representative conformer: 1 |