+
Open data
-
Basic information
Entry | Database: PDB / ID: 1i13 | ||||||
---|---|---|---|---|---|---|---|
Title | ANALYSIS OF AN INVARIANT ASPARTIC ACID IN HPRTS-ALANINE 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 |
| ||||||
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. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 93.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 70.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 19.1 KB | Display | |
Data in CIF | ![]() | 26.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1i0iC ![]() 1i0lC ![]() 1i14C ![]() 1tc2S S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
-Protein / Sugars , 2 types, 4 molecules AB![](data/chem/img/PRP.gif)
![](data/chem/img/PRP.gif)
#1: Protein | Mass: 25480.316 Da / Num. of mol.: 2 / Mutation: M23K, S66C, V86L, D115A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q27796, UniProt: Q4DRC4*PLUS, hypoxanthine phosphoribosyltransferase #4: Sugar | |
---|
-Non-polymers , 4 types, 185 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/7HP.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/7HP.gif)
![](data/chem/img/FMT.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #3: Chemical | #5: Chemical | ChemComp-FMT / | #6: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.06 % |
---|---|
Crystal grow | 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 |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 21, 1999 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→30 Å / Num. obs: 36405 / % possible obs: 95.8 % / Observed criterion σ(I): -3 / Redundancy: 2.3 % / Rmerge(I) obs: 0.056 / Net I/σ(I): 13.7 |
Reflection shell | Resolution: 1.8→1.84 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 2.3 / % possible all: 92.5 |
Reflection | *PLUS Num. obs: 33269 |
Reflection shell | *PLUS Highest resolution: 1.84 Å / Lowest resolution: 1.89 Å / % possible obs: 93.7 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 2.9 |
-
Processing
Software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: pdb entry 1tc2 with ligands, water molecules and loop II removed Resolution: 1.84→6 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber Details: PATCH STATEMENTS WERE USED FOR CIS PEPTIDES AND METAL-OXYGEN BONDS
| ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.84→6 Å
| ||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||
LS refinement shell | Resolution: 1.8→1.84 Å / Total num. of bins used: 15
| ||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.25 / Rfactor obs: 0.192 | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor obs: 0.271 |