+Open data
-Basic information
Entry | Database: PDB / ID: 1gai | |||||||||
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Title | GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE | |||||||||
Components | GLUCOAMYLASE-471 | |||||||||
Keywords | HYDROLASE / GLYCOSIDASE / POLYSACCHARIDE DEGRADATION / GLYCOPROTEIN | |||||||||
Function / homology | Function and homology information glucan 1,4-alpha-glucosidase / glucan 1,4-alpha-glucosidase activity / starch binding / polysaccharide catabolic process Similarity search - Function | |||||||||
Biological species | Aspergillus awamori (mold) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | |||||||||
Authors | Aleshin, A.E. / Stoffer, B. / Firsov, L.M. / Svensson, B. / Honzatko, R.B. | |||||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism. Authors: Aleshin, A.E. / Stoffer, B. / Firsov, L.M. / Svensson, B. / Honzatko, R.B. #1: Journal: FEBS Lett. / Year: 1995 Title: Refined Structure for the Complex of D-Gluco-Dihydroacarbose with Glucoamylase from Aspergillus Awamori Var. X100 to 2.2 A Resolution: Dual Conformations for Extended Inhibitors Bound to the ...Title: Refined Structure for the Complex of D-Gluco-Dihydroacarbose with Glucoamylase from Aspergillus Awamori Var. X100 to 2.2 A Resolution: Dual Conformations for Extended Inhibitors Bound to the Active Site of Glucoamylase Authors: Stoffer, B. / Aleshin, A.E. / Firsov, L.M. / Svensson, B. / Honzatko, R.B. #2: Journal: J.Mol.Biol. / Year: 1994 Title: Refined Crystal Structures of Glucoamylase from Aspergillus Awamori Var. X100 Authors: Aleshin, A.E. / Hoffman, C. / Firsov, L.M. / Honzatko, R.B. #3: Journal: J.Biol.Chem. / Year: 1994 Title: Refined Structure for the Complex of Acarbose with Glucoamylase from Aspergillus Awamori Var. X100 to 2.4-A Resolution Authors: Aleshin, A.E. / Firsov, L.M. / Honzatko, R.B. #4: Journal: Biochemistry / Year: 1993 Title: Refined Structure for the Complex of 1-Deoxynojirimycin with Glucoamylase from Aspergillus Awamori Var. X100 to 2.4-A Resolution Authors: Harris, E.M. / Aleshin, A.E. / Firsov, L.M. / Honzatko, R.B. #5: Journal: J.Biol.Chem. / Year: 1992 Title: Crystal Structure of Glucoamylase from Aspergillus Awamori Var. X100 to 2.2-A Resolution Authors: Aleshin, A. / Golubev, A. / Firsov, L.M. / Honzatko, R.B. | |||||||||
History |
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Remark 700 | SHEET MOST OF THE SHEETS FOR GLUCOAMYLASE-471 ARE HAIRPIN LOOPS THAT CONNECT HELICES. THESE LOOPS ...SHEET MOST OF THE SHEETS FOR GLUCOAMYLASE-471 ARE HAIRPIN LOOPS THAT CONNECT HELICES. THESE LOOPS HAVE TWO OR MORE H-BONDS BETWEEN THE ANTIPARALLEL STRANDS THAT COMPRISE THEM. IN ADDITION INDIVIDUAL LOOPS PACK TOGETHER, BUT THERE EXISTS GENERALLY ONLY ONE H-BOND BETWEEN A LOOP AND ITS NEIGHBOR. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gai.cif.gz | 171.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gai.ent.gz | 141.7 KB | Display | PDB format |
PDBx/mmJSON format | 1gai.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ga/1gai ftp://data.pdbj.org/pub/pdb/validation_reports/ga/1gai | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein / Non-polymers , 2 types, 552 molecules A
#1: Protein | Mass: 50608.883 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-471 / Source method: isolated from a natural source / Details: COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE / Source: (natural) Aspergillus awamori (mold) / Variant: X100 References: UniProt: P22832, UniProt: P69327*PLUS, glucan 1,4-alpha-glucosidase |
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#6: Water | ChemComp-HOH / |
-Sugars , 4 types, 13 molecules
#2: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Polysaccharide | 4,6-dideoxy-4-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}-alpha-D- ...4,6-dideoxy-4-{[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / dihydro-alpha-acarbose |
#5: Sugar | ChemComp-MAN / |
-Details
Compound details | GLUCOAMYLASE-471 IS A NATURAL PROTEOLYTIC FRAGMENT OF PARENT GLUCOAMYLASE, WHICH IS INITIALLY ...GLUCOAMYLA |
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Nonpolymer details | D-GLUCO-DIHYDROACARBOSE IS BOUND TO THE ACTIVE SITE OF THE ENZYME. D-GLUCO-DIHYDROACARBOSE IS A ...D-GLUCO-DIHYDROACA |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.1 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 4 / Details: pH 4. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop / Details: Golubev, A. M., (1992) J. Mol. Biol., 226, 271. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Oct 20, 1993 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→30 Å / Num. obs: 64147 / % possible obs: 96 % / Observed criterion σ(I): 4 / Redundancy: 4.66 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 36.16 |
Reflection shell | Resolution: 1.69→1.8 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.257 / Mean I/σ(I) obs: 3.3 / % possible all: 75.5 |
Reflection | *PLUS Num. obs: 64713 / Num. measured all: 298712 |
Reflection shell | *PLUS Highest resolution: 1.7 Å / % possible obs: 75 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: NATIVE GLOCOAMYLASE Resolution: 1.7→10 Å / σ(F): 1
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Displacement parameters | Biso mean: 14.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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