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- PDB-1kul: GLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, 5 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1kul
TitleGLUCOAMYLASE, GRANULAR STARCH-BINDING DOMAIN, NMR, 5 STRUCTURES
ComponentsGLUCOAMYLASE
KeywordsHYDROLASE / STARCH BINDING DOMAIN
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
Glucoamylase, starch-binding / Glucoamylase, CBM20 domain / Glucoamylase / : / Glucoamylase active site region signature. / GH15-like domain / Glycosyl hydrolases family 15 / Carbohydrate binding module family 20 / Starch binding domain / CBM20 (carbohydrate binding type-20) domain profile. ...Glucoamylase, starch-binding / Glucoamylase, CBM20 domain / Glucoamylase / : / Glucoamylase active site region signature. / GH15-like domain / Glycosyl hydrolases family 15 / Carbohydrate binding module family 20 / Starch binding domain / CBM20 (carbohydrate binding type-20) domain profile. / Starch binding domain / Carbohydrate-binding-like fold / Six-hairpin glycosidase-like superfamily / Six-hairpin glycosidase superfamily / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesAspergillus niger (mold)
MethodSOLUTION NMR
AuthorsSorimachi, K. / Jacks, A.J. / Le Gal-Coeffet, M.-F. / Williamson, G. / Archer, D.B. / Williamson, M.P.
Citation
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.
#1: 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
DepositionJan 12, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GLUCOAMYLASE


Theoretical massNumber of molelcules
Total (without water)11,8851
Polymers11,8851
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)5 / 100
Representative

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Components

#1: Protein GLUCOAMYLASE / 1 / 4-ALPHA-D-GLUCAN GLUCOHYDROLASE


Mass: 11884.820 Da / Num. of mol.: 1 / Fragment: BINDING DOMAIN, RESIDUES 509 - 616
Source method: isolated from a genetically manipulated source
Details: PH 5.2, 313 K / Source: (gene. exp.) Aspergillus niger (mold) / Strain: AB4.1 / Gene: A. NIGER GLAA / Plasmid: PIGF / Gene (production host): A. NIGER GLAA / Production host: Aspergillus niger (mold) / References: UniProt: P69328, glucan 1,4-alpha-glucosidase
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 5.2 / Temperature: 313 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers calculated total number: 100 / Conformers submitted total number: 5

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