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- PDB-1pl0: Crystal structure of human ATIC in complex with folate-based inhi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pl0 | ||||||
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Title | Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC | ||||||
![]() | Bifunctional purine biosynthesis protein PURH | ||||||
![]() | TRANSFERASE / HYDROLASE / human ATIC / AICAR / AICAR transformylase / IMP Cyclohydrolase / xanthosine monophosphate / folate-based inhibitor / BW2315U89UC | ||||||
Function / homology | ![]() phosphoribosylaminoimidazolecarboxamide formyltransferase / phosphoribosylaminoimidazolecarboxamide formyltransferase activity / IMP cyclohydrolase / IMP cyclohydrolase activity / 'de novo' XMP biosynthetic process / brainstem development / Purine ribonucleoside monophosphate biosynthesis / 'de novo' AMP biosynthetic process / GMP biosynthetic process / cellular response to interleukin-7 ...phosphoribosylaminoimidazolecarboxamide formyltransferase / phosphoribosylaminoimidazolecarboxamide formyltransferase activity / IMP cyclohydrolase / IMP cyclohydrolase activity / 'de novo' XMP biosynthetic process / brainstem development / Purine ribonucleoside monophosphate biosynthesis / 'de novo' AMP biosynthetic process / GMP biosynthetic process / cellular response to interleukin-7 / nucleobase-containing compound metabolic process / 'de novo' IMP biosynthetic process / dihydrofolate metabolic process / : / animal organ regeneration / tetrahydrofolate biosynthetic process / cerebellum development / cerebral cortex development / Signaling by ALK fusions and activated point mutants / cadherin binding / protein homodimerization activity / extracellular exosome / membrane / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cheong, C.G. / Greasley, S.E. / Horton, P.A. / Beardsley, G.P. / Wilson, I.A. | ||||||
![]() | ![]() Title: Crystal Structures of Human Bifunctional Enzyme Aminoimidazole-4-carboxamide Ribonucleotide Transformylase/IMP Cyclohydrolase in Complex with Potent Sulfonyl-containing Antifolates. Authors: Cheong, C.G. / Wolan, D.W. / Greasley, S.E. / Horton, P.A. / Beardsley, G.P. / Wilson, I.A. | ||||||
History |
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Remark 600 | HETEROGEN PART OF THE BW2 LIGAND IS MISSING DUE TO LACK OF ELECTRON DENSITY. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 449.7 KB | Display | ![]() |
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PDB format | ![]() | 363.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.5 MB | Display | ![]() |
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Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 89 KB | Display | |
Data in CIF | ![]() | 120.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1p4rC ![]() 1g8mS C: citing same article ( S: Starting model for refinement |
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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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2 | ![]()
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Unit cell |
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Details | Biological unit is a homodimer |
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 64693.719 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: INCLUDES: PHOSPHORIBOSYLAMINOIMIDAZOLECARBOXAMIDE FORMYLTRANSFERASE (AICAR TRANSFORMYLASE) AND IMP CYCLOHYDROLASE (INOSINICASE) (IMP SYNTHETASE) Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P31939, phosphoribosylaminoimidazolecarboxamide formyltransferase, IMP cyclohydrolase |
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-Non-polymers , 5 types, 399 molecules ![](data/chem/img/K.gif)
![](data/chem/img/XMP.gif)
![](data/chem/img/AMZ.gif)
![](data/chem/img/BW2.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/XMP.gif)
![](data/chem/img/AMZ.gif)
![](data/chem/img/BW2.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-K / #3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.23 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: polyethylene glycol 3000, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 106 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. obs: 71039 / % possible obs: 91.3 % / Redundancy: 2.7 % / Rsym value: 0.124 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 2.6→2.64 Å / Redundancy: 2.4 % / Mean I/σ(I) obs: 1.5 / Num. unique all: 3597 / Rsym value: 0.659 / % possible all: 92.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1G8M Resolution: 2.6→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
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Refine LS restraints |
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