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- PDB-1lor: crystal structure of orotidine 5'-monophosphate complexed with BMP -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lor | ||||||
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Title | crystal structure of orotidine 5'-monophosphate complexed with BMP | ||||||
![]() | orotidine monophosphate decarboxylase | ||||||
![]() | LYASE / TIM barrel | ||||||
Function / homology | ![]() orotidine-5'-phosphate decarboxylase / orotidine-5'-phosphate decarboxylase activity / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wu, N. / Pai, E.F. | ||||||
![]() | ![]() Title: Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase. Authors: Wu, N. / Pai, E.F. | ||||||
History |
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Remark 999 | sequence Authors state that although residue 1 is MET and residue 101 is Arg according to the ... sequence Authors state that although residue 1 is MET and residue 101 is Arg according to the SwissProt entry, residue 1 was LEU and residue 101 was Pro in the original construct cloned of MT genomic dna. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.6 KB | Display | ![]() |
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PDB format | ![]() | 40.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 754.9 KB | Display | ![]() |
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Full document | ![]() | 755.2 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 17.2 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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Details | The second part of the biological dimer can be generated by the two fold axis -x, y, -z+1/2 |
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Components
#1: Protein | Mass: 24866.658 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pET15b / Production host: ![]() ![]() References: UniProt: O26232, orotidine-5'-phosphate decarboxylase |
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#2: Chemical | ChemComp-BMP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.26 % | ||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: trisodium citrate, dioxane, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 25K | ||||||||||||||||||
Crystal grow | *PLUS PH range low: 8.5 / PH range high: 6.5 | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→30 Å / Num. all: 28942 / Num. obs: 28942 / % possible obs: 97 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 14.4 Å2 |
Reflection shell | Resolution: 1.6→1.63 Å / % possible all: 92.8 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 97 % / Num. measured all: 355820 / Rmerge(I) obs: 0.03 |
Reflection shell | *PLUS % possible obs: 92.8 % / Rmerge(I) obs: 0.085 |
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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: 47.7627 Å2 / ksol: 0.394807 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15 Å2
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Refine analyze | Luzzati coordinate error free: 0.17 Å / Luzzati sigma a free: 0.04 Å | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→29.88 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.7 Å / Rfactor Rfree error: 0.011 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 30 Å / Rfactor all: 0.173 / Rfactor Rfree: 0.196 / Rfactor Rwork: 0.173 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 1.7 Å / Rfactor Rfree: 0.208 / Rfactor Rwork: 0.161 |