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- PDB-1knj: Co-Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosph... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1knj | ||||||
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Title | Co-Crystal Structure of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate Synthase (ispF) from E. coli Involved in Mevalonate-Independent Isoprenoid Biosynthesis, Complexed with CMP/MECDP/Mn2+ | ||||||
![]() | 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||||
![]() | METAL BINDING PROTEIN / isoprenoids / deoxyxylulose/methyl-erythritol-phosphate pathway / cyclodiphosphate / MEP / YgbB / ispF / MECDP / 2-C-methyl-D-erythritol-2 / 4-cyclodiphosphate synthase | ||||||
Function / homology | ![]() 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity / ubiquinone biosynthetic process / isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / terpenoid biosynthetic process / manganese ion binding / zinc ion binding / identical protein binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Richard, S.B. / Ferrer, J.L. / Bowman, M.E. / Lillo, A.M. / Tetzlaff, C.N. / Cane, D.E. / Noel, J.P. | ||||||
![]() | ![]() Title: Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway. Authors: Richard, S.B. / Ferrer, J.L. / Bowman, M.E. / Lillo, A.M. / Tetzlaff, C.N. / Cane, D.E. / Noel, J.P. #1: ![]() Title: Structure of 4-diphosphocytidyl-2-C-methylerythritol Synthetase Involved in Mevalonate-Independent Isoprenoid Biosynthesis Authors: Richard, S.B. / Bowman, M.E. / Kwiatkowski, W. / Kang, I. / Chow, C. / Lillo, A.M. / Cane, D.E. / Noel, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 40.8 KB | Display | ![]() |
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PDB format | ![]() | 32.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 9.5 KB | Display | |
Data in CIF | ![]() | 11.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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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Components on special symmetry positions |
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Details | The biological assembly is a homotrimer generated from the monomer in the asymmetric unit by the operations: z,x,y and y,z,x |
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Components
#1: Protein | Mass: 17108.113 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MN / |
#3: Chemical | ChemComp-C5P / |
#4: Chemical | ChemComp-CDI / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: (NH4)2SO4, PEG 400, NaI, PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 26, 2001 / Details: mirrors | ||||||||||||||||||
Radiation |
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Radiation wavelength |
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Reflection | Resolution: 2.7→99 Å / Num. all: 11923 / Num. obs: 11923 / % possible obs: 99.3 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4.1 % / Biso Wilson estimate: 92 Å2 / Rmerge(I) obs: 0.04 / Rsym value: 0.066 / Net I/σ(I): 19 | ||||||||||||||||||
Reflection shell | Resolution: 2.8→2.87 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.66 / Mean I/σ(I) obs: 482 / Num. unique all: 1579 / % possible all: 100 | ||||||||||||||||||
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 99 Å / Num. obs: 24118 / Num. measured all: 96785 / Rmerge(I) obs: 0.066 | ||||||||||||||||||
Reflection shell | *PLUS % possible obs: 100 % / Rmerge(I) obs: 0.66 / Mean I/σ(I) obs: 1.2 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 41.9833 Å2 / ksol: 0.333926 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 62.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→14.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.98 Å / Rfactor Rfree error: 0.038 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.8 Å / % reflection Rfree: 5 % / Rfactor all: 0.286 / Rfactor Rfree: 0.258 / Rfactor Rwork: 0.23 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.37 / Rfactor Rwork: 0.334 |