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Open data
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Basic information
Entry | Database: PDB / ID: 2car | ||||||
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Title | Crystal Structure Of Human Inosine Triphosphatase | ||||||
![]() | INOSINE TRIPHOSPHATE PYROPHOSPHATASE | ||||||
![]() | HYDROLASE / INOSINE TRIPHOSPHATE PYROPHOSPHOHYDROLASE / INOSINE TRIPHOSPHATASE DEFICIENCY / ITP / IMP / DISEASE MUTATION / NUCLEOTIDE METABOLISM | ||||||
Function / homology | ![]() ITP catabolic process / deoxyribonucleoside triphosphate catabolic process / ITP diphosphatase activity / XTP diphosphatase activity / dITP diphosphatase activity / nucleotide diphosphatase / nucleoside triphosphate catabolic process / nucleoside triphosphate diphosphatase activity / Ribavirin ADME / Purine catabolism ...ITP catabolic process / deoxyribonucleoside triphosphate catabolic process / ITP diphosphatase activity / XTP diphosphatase activity / dITP diphosphatase activity / nucleotide diphosphatase / nucleoside triphosphate catabolic process / nucleoside triphosphate diphosphatase activity / Ribavirin ADME / Purine catabolism / chromosome organization / intracellular membrane-bounded organelle / nucleotide binding / nucleoplasm / identical protein binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Stenmark, P. / Kursula, P. / Arrowsmith, C. / Berglund, H. / Edwards, A. / Ehn, M. / Flodin, S. / Flores, A. / Graslund, S. / Hammarstrom, M. ...Stenmark, P. / Kursula, P. / Arrowsmith, C. / Berglund, H. / Edwards, A. / Ehn, M. / Flodin, S. / Flores, A. / Graslund, S. / Hammarstrom, M. / Hallberg, B.M. / Hogbom, M. / Holmberg Schiavone, L. / Kotenyova, T. / Nilsson-Ehle, P. / Nyman, T. / Ogg, D. / Persson, C. / Sagemark, J. / Schuler, H. / Sundstrom, M. / Thorsell, A.G. / van den Berg, S. / Weigelt, J. / Nordlund, P. | ||||||
![]() | ![]() Title: Crystal Structure of Human Inosine Triphosphatase. Substrate Binding and Implication of the Inosine Triphosphatase Deficiency Mutation P32T. Authors: Stenmark, P. / Kursula, P. / Flodin, S. / Graslund, S. / Landry, R. / Nordlund, P. / Schuler, H. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 199.4 KB | Display | ![]() |
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PDB format | ![]() | 160.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.8 KB | Display | ![]() |
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Full document | ![]() | 450.4 KB | Display | |
Data in XML | ![]() | 24.2 KB | Display | |
Data in CIF | ![]() | 37.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2j4eC ![]() 1b78S S: Starting model for refinement C: citing same article ( |
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Similar 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.99999, -0.00266, 0.00228), Vector: |
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Components
#1: Protein | Mass: 21612.756 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9BY32, nucleoside-triphosphate diphosphatase #2: Water | ChemComp-HOH / | Compound details | HYDROLYZES | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35 % Description: THE CRYSTAL WAS PSEUDO MEROHEDRALLY TWINNED. THE TWINNING OPERATION IS -K,-H, L. THE TWINNING FRACTION IS 0.50. THE TEST SET IS NOT RELATED TO THE WORKING SET BY THE TWIN OPERATION. |
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Crystal grow | Details: 0.2 M POTASSIUM CHLORIDE, 27 % (W/V) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 22, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9781 Å / Relative weight: 1 |
Reflection | Resolution: 1.09→40 Å / Num. obs: 123899 / % possible obs: 92.5 % / Redundancy: 4.6 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 18.8 |
Reflection shell | Resolution: 1.09→1.2 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 4.8 / % possible all: 86.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1B78 Resolution: 1.09→40 Å / Num. parameters: 35184 / Num. restraintsaints: 45253 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Refine analyze | Num. disordered residues: 35 / Occupancy sum hydrogen: 2881 / Occupancy sum non hydrogen: 3674.5 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.09→40 Å
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Refine LS restraints |
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