+Open data
-Basic information
Entry | Database: PDB / ID: 2rts | ||||||
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Title | Chitin binding domain1 | ||||||
Components | chitinase | ||||||
Keywords | HYDROLASE / chitin binding domain | ||||||
Function / homology | Function and homology information chitin binding / hydrolase activity, hydrolyzing O-glycosyl compounds / carbohydrate binding / carbohydrate metabolic process / extracellular region Similarity search - Function | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Uegaki, K. | ||||||
Citation | Journal: J.Biochem. / Year: 2014 Title: Solution structure of the chitin-binding domain 1 (ChBD1) of a hyperthermophilic chitinase from Pyrococcus furiosus. Authors: Mine, S. / Nakamura, T. / Sato, T. / Ikegami, T. / Uegaki, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rts.cif.gz | 760 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rts.ent.gz | 653.7 KB | Display | PDB format |
PDBx/mmJSON format | 2rts.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rt/2rts ftp://data.pdbj.org/pub/pdb/validation_reports/rt/2rts | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8352.068 Da / Num. of mol.: 1 / Fragment: chitin binding domain, UNP RESIDUES 65-135 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 / Gene: PF1234 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8U1H4 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR / Details: NMR structure of chitin binding domain1 | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM [U-100% 15N] MES-1, 1 mM [U-100% 13C; U-100% 15N] MES-2, 1 mM MES-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 30 / Representative conformer: 1 |