+Open data
-Basic information
Entry | Database: PDB / ID: 1amy | ||||||
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Title | CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE | ||||||
Components | 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE | ||||||
Keywords | HYDROLASE (O-GLYCOSYL) | ||||||
Function / homology | Function and homology information starch catabolic process / alpha-amylase / alpha-amylase activity / calcium ion binding Similarity search - Function | ||||||
Biological species | Hordeum vulgare (barley) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Kadziola, A. / Haser, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Crystal and molecular structure of barley alpha-amylase. Authors: Kadziola, A. / Abe, J. / Svensson, B. / Haser, R. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Characterization, Crystallization and Crystallographic Preliminary Data of the Complex between Barley Alpha-Amylase and the Bifunctional Alpha-Amylase(Slash)Subtilisin Inhibitor from Barley Seeds Authors: Vallee, F. / Kadziola, A. / Bourne, Y. / Abe, J.-I. / Svensson, B. / Haser, R. #2: Journal: J.Biol.Chem. / Year: 1993 Title: Site-Directed Mutagenesis of Histidine 93, Aspartic Acid 180, Glutamic Acid 20 5, Histidine 290, and Aspartic Acid 291 at the Active Site and Tryptophan 279 at the Raw Starch Binding Site in Barley Alpha-Amylase 1 Authors: Sogaard, M. / Kadziola, A. / Haser, R. / Svensson, B. | ||||||
History |
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Remark 700 | SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1amy.cif.gz | 96.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1amy.ent.gz | 72.9 KB | Display | PDB format |
PDBx/mmJSON format | 1amy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/am/1amy ftp://data.pdbj.org/pub/pdb/validation_reports/am/1amy | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 129 |
-Components
#1: Protein | Mass: 44986.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hordeum vulgare (barley) / References: UniProt: P04063, alpha-amylase | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE STRUCTURE CAN BE DESCRIBED AS CONSISTING OF THREE DOMAINS: A CENTRAL DOMAIN (A) FORMING AN ...THE STRUCTURE CAN BE DESCRIBED AS CONSISTING | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.67 Å3/Da / Density % sol: 73.64 % | ||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 75 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.77 Å / Num. obs: 19542 / % possible obs: 89 % / Num. measured all: 109747 / Rmerge(I) obs: 0.151 |
-Processing
Software |
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Refinement | Resolution: 2.8→10 Å / σ(F): 1 Details: IN A FINAL 2FOBS-FCALC MAP NO DENSITY WAS SEEN FOR THE SIDE CHAINS OF LYS 158, TYR 378, AND LYS 389.
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Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.92 Å / Num. reflection obs: 1386 / Rfactor obs: 0.233 |