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Open data
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Basic information
Entry | Database: PDB / ID: 1i0i | ||||||
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Title | ANALYSIS OF AN INVARIANT ASPARTIC ACID IN HPRTS-GLUTAMINE MUTANT | ||||||
![]() | HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE | ||||||
![]() | TRANSFERASE / PHOSPHORIBOSYLTRANSFERASE / NUCLEOTIDE METABOLISM / PURINE SALVAGE / TERNARY COMPLEX / CATALYTIC BASE | ||||||
Function / homology | ![]() hypoxanthine phosphoribosyltransferase / guanine salvage / hypoxanthine metabolic process / guanine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase activity / GMP salvage / IMP salvage / purine ribonucleoside salvage / nucleotide binding / magnesium ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Canyuk, B. / Focia, P.J. / Eakin, A.E. | ||||||
![]() | ![]() Title: The role for an invariant aspartic acid in hypoxanthine phosphoribosyltransferases is examined using saturation mutagenesis, functional analysis, and X-ray crystallography. Authors: Canyuk, B. / Focia, P.J. / Eakin, A.E. #1: ![]() Title: Approaching the Transition State in the Crystal Structure of a Phosphoribosyltransferase Authors: Focia, P.J. / Craig, S.P. / Eakin, A.E. | ||||||
History |
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Remark 999 | SEQUENCE THIS HPRT WAS CLONED FROM A DIFFERENT STRAIN OF TRYPANOSOMA CRUZI AND VARIES FROM A ...SEQUENCE THIS HPRT WAS CLONED FROM A DIFFERENT STRAIN OF TRYPANOSOMA CRUZI AND VARIES FROM A PREVIOUSLY REPORTED SEQUENCE AT LYS 23, CYS 66 AND LEU 86. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 94.6 KB | Display | ![]() |
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PDB format | ![]() | 71.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1i0lC ![]() 1i13C ![]() 1i14C ![]() 1tc2S 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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Unit cell |
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Components
#1: Protein | Mass: 25537.367 Da / Num. of mol.: 2 / Mutation: M23K, S66C, V86L, D115Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q27796, UniProt: Q4DRC4*PLUS, hypoxanthine phosphoribosyltransferase #2: Chemical | ChemComp-MG / #3: Chemical | #4: Sugar | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.84 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: PEG 6000, Sodium acetate, Ammonium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jul 25, 1998 |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.06→30 Å / Num. obs: 22986 / % possible obs: 92.1 % / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Rmerge(I) obs: 0.068 / Rsym value: 0.068 / Net I/σ(I): 17.3 |
Reflection shell | Resolution: 2.06→2.11 Å / Redundancy: 4 % / Rmerge(I) obs: 0.411 / % possible all: 56.2 |
Reflection | *PLUS Num. obs: 21963 |
Reflection shell | *PLUS % possible obs: 56.2 % / Mean I/σ(I) obs: 2.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1tc2 with ligands, waters and loop II removed Resolution: 2.06→6 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: PATCH STATEMENTS WERE USED FOR CIS PEPTIDES AND METAL-OXYGEN BONDS
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Refinement step | Cycle: LAST / Resolution: 2.06→6 Å
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Refine LS restraints |
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Xplor file |
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Refinement | *PLUS Rfactor all: 0.25 / Rfactor obs: 0.168 | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS |