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- PDB-6enl: INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6enl | ||||||
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Title | INHIBITION OF ENOLASE: THE CRYSTAL STRUCTURES OF ENOLASE-CA2+-PHOSPHOGLYCERATE AND ENOLASE-ZN2+-PHOSPHOGLYCOLATE COMPLEXES AT 2.2-ANGSTROMS RESOLUTION | ||||||
![]() | ENOLASE | ||||||
![]() | CARBON-OXYGEN LYASE | ||||||
Function / homology | ![]() Gluconeogenesis / regulation of vacuole fusion, non-autophagic / Glycolysis / melatonin binding / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / fungal-type vacuole / glycolytic process / magnesium ion binding ...Gluconeogenesis / regulation of vacuole fusion, non-autophagic / Glycolysis / melatonin binding / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / fungal-type vacuole / glycolytic process / magnesium ion binding / mitochondrion / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lebioda, L. / Stec, B. | ||||||
![]() | ![]() Title: Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution. Authors: Lebioda, L. / Stec, B. / Brewer, J.M. / Tykarska, E. #1: ![]() Title: Mechanism of Enolase: The Crystal Structure of Enolase-Mg2+-Phosphoglycerate(Slash) Phosphoenolpyruvate Complex at 2.2-Angstroms Resolution Authors: Lebioda, L. / Stec, B. #2: ![]() Title: Refined Structure of Yeast Apo-Enolase at 2.25 Angstroms Resolution Authors: Stec, B. / Lebioda, L. #3: ![]() Title: Crystal Structure of Holoenzyme Refined at 1.9 Angstroms Resolution: Trigonal-Bipyramidal Geometry of the Cation Binding Site Authors: Lebioda, L. / Stec, B. #4: ![]() Title: The Structure of Yeast Enolase at 2.25-Angstroms Resolution. An 8-Fold Beta+Alpha-Barrel with a Novel Beta Beta Alpha Alpha (Beta Alpha)6 Topology Authors: Lebioda, L. / Stec, B. / Brewer, J.M. #5: ![]() Title: Crystal Structure of Enolase Indicates that Enolase and Pyruvate Kinase Evolved from a Common Ancestor Authors: Lebioda, L. / Stec, B. #6: ![]() Title: Crystallization and Preliminary Crystallographic Data for a Tetragonal Form of Yeast Enolase Authors: Lebioda, L. / Brewer, J.M. | ||||||
History |
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Remark 700 | SHEET THE SHEET PRESENTED AS *BAR* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *BAR* 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. THERE IS A SMALL STRAND BONDED TO THE END OF STRAND 1 OF THE BARREL. THIS SMALL STRAND STRAND AND STRAND 1 ARE PRESENTED AS SHEET S1. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 103 KB | Display | ![]() |
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PDB format | ![]() | 78.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO 143 AND PRO 265 ARE CIS PROLINES. 2: RESIDUES GLY 41 - VAL 42 AND PRO 265 - LYS 269 ARE PROBABLY PARTIALLY DISORDERED. |
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Components
#1: Protein | Mass: 46690.691 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P00924, phosphopyruvate hydratase |
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#2: Chemical | ChemComp-PGA / |
#3: Chemical | ChemComp-ZN / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.39 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.2 Å / Num. obs: 25431 / Num. measured all: 51668 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.157 / Highest resolution: 2.2 Å Details: RESIDUES GLY 41 - VAL 42 AND PRO 265 - LYS 269 ARE PROBABLY PARTIALLY DISORDERED. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / Num. reflection obs: 18279 / σ(F): 3 / Rfactor obs: 0.157 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |