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- PDB-2ada: ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ada | |||||||||
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Title | ATOMIC STRUCTURE OF ADENOSINE DEAMINASE COMPLEXED WITH A TRANSITION-STATE ANALOG: UNDERSTANDING CATALYSIS AND IMMUNODEFICIENCY MUTATIONS | |||||||||
![]() | ADENOSINE DEAMINASE![]() | |||||||||
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Function / homology | ![]() mature B cell apoptotic process / xanthine biosynthetic process / negative regulation of penile erection / Purine salvage / Ribavirin ADME / negative regulation of circadian sleep/wake cycle, non-REM sleep / negative regulation of mucus secretion / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Wilson, D.K. / Quiocho, F.A. | |||||||||
![]() | ![]() Title: Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Authors: Wilson, D.K. / Rudolph, F.B. / Quiocho, F.A. #1: ![]() Title: Crystallographic Observation of a Trapped Tetrahedral Intermediate in a Metalloenzyme Authors: Wilson, D.K. / Quiocho, F.A. #2: ![]() Title: A Pre-Transition-State Mimic of an Enzyme: X-Ray Structure of Adenosine Deaminase with Bound 1-Deazaadenosine Authors: Wilson, D.K. / Quiocho, F.A. #3: ![]() Title: Refined 2.5 Angstroms Structure of the Murine Adenosine Deaminase at Ph 6.0 Authors: Sharff, A.J. / Wilson, D.K. / Chang, Z. #4: ![]() Title: Preliminary X-Ray Analysis of Crystals of Murine Adenosine Deaminase Authors: Wilson, D.K. / Rudolph, F.B. / Harrison, M.L. / Kellems, R.E. / Quiocho, F.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.7 KB | Display | ![]() |
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PDB format | ![]() | 62.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 40045.590 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-HPR / |
#4: Water | ChemComp-HOH / ![]() |
Nonpolymer details | COMPND LIGAND IS FORMED IN ENZYME ACTIVE SITE FROM PURINE RIBOSIDE. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.49 Å3/Da / Density % sol: 64.78 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 4.2 / Method: vapor diffusion / Details: Wilson, D.K., (1988) J.Mol.Biol., 200, 613. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | Num. obs: 20445 / % possible obs: 93 % / Observed criterion σ(F): 3 |
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Reflection | *PLUS Highest resolution: 2.4 Å / Num. measured all: 72059 / Rmerge(I) obs: 0.0324 |
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Processing
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Refinement | Resolution: 2.4→10 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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