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Yorodumi- PDB-1acz: GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1acz | |||||||||
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Title | GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN COMPLEX WITH CYCLODEXTRIN, NMR, 5 STRUCTURES | |||||||||
Components | GLUCOAMYLASE | |||||||||
Keywords | POLYSACCHARIDE DEGRADATION / HYDROLASE / STARCH BINDING DOMAIN / GLYCOSIDASE / GLYCOPROTEIN / ALTERNATIVE SPLICING | |||||||||
Function / homology | Function and homology information glucan 1,4-alpha-glucosidase / polysaccharide metabolic process / glucan 1,4-alpha-glucosidase activity / starch binding / fungal-type vacuole / polysaccharide catabolic process / endoplasmic reticulum Similarity search - Function | |||||||||
Biological species | Aspergillus niger (mold) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Sorimachi, K. / Le Gal-Coeffet, M.-F. / Williamson, G. / Archer, D.B. / Williamson, M.P. | |||||||||
Citation | Journal: Structure / Year: 1997 Title: Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Authors: Sorimachi, K. / Le Gal-Coeffet, M.F. / Williamson, G. / Archer, D.B. / Williamson, M.P. #1: Journal: J.Mol.Biol. / Year: 1996 Title: Solution Structure of the Granular Starch Binding Domain of Glucoamylase from Aspergillus Niger by Nuclear Magnetic Resonance Spectroscopy Authors: Sorimachi, K. / Jacks, A.J. / Le Gal-Coeffet, M.F. / Williamson, G. / Archer, D.B. / Williamson, M.P. #2: Journal: Eur.J.Biochem. / Year: 1995 Title: 1H and 15N Assignments and Secondary Structure of the Starch-Binding Domain of Glucoamylase from Aspergillus Niger Authors: Jacks, A.J. / Sorimachi, K. / Le Gal-Coeffet, M.F. / Williamson, G. / Archer, D.B. / Williamson, M.P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1acz.cif.gz | 179.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1acz.ent.gz | 148.3 KB | Display | PDB format |
PDBx/mmJSON format | 1acz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1acz_validation.pdf.gz | 583.1 KB | Display | wwPDB validaton report |
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Full document | 1acz_full_validation.pdf.gz | 758 KB | Display | |
Data in XML | 1acz_validation.xml.gz | 43.7 KB | Display | |
Data in CIF | 1acz_validation.cif.gz | 55.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ac/1acz ftp://data.pdbj.org/pub/pdb/validation_reports/ac/1acz | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11884.820 Da / Num. of mol.: 1 / Fragment: STARCH-BINDING DOMAIN, RESIDUES 509 - 616 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus niger (mold) / Strain: AB4.1 / Plasmid: PIGF / Gene (production host): GLAA / Production host: Aspergillus niger (mold) References: UniProt: P04064, UniProt: P69328*PLUS, glucan 1,4-alpha-glucosidase |
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#2: Polysaccharide |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 5.7 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 500 / Manufacturer: Bruker / Model: AMX 500 / Field strength: 500 MHz |
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-Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: RANDOM FROM 81 GOOD STRUCTURES Conformers calculated total number: 100 / Conformers submitted total number: 5 |