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- PDB-1cni: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWOR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cni | ||||||
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Title | X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE | ||||||
![]() | CARBONIC ANHYDRASE II![]() | ||||||
![]() | LYASE (OXO-ACID) | ||||||
Function / homology | ![]() positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lesburg, C.A. / Christianson, D.W. | ||||||
![]() | Journal: J.Am.Chem.Soc. / Year: 1995 Title: X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in a Protein-Zinc Binding Site Authors: Lesburg, C.A. / Christianson, D.W. #1: ![]() Title: Hydrogen Bond Network in the Metal Binding Site of Carbonic Anhydrase Enhances Zinc Affinity and Catalytic Efficiency Authors: Kiefer, L.L. / Paterno, S.A. / Fierke, C.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 | ![]() | 68.5 KB | Display | ![]() |
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PDB format | ![]() | 49.4 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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Atom site foot note | 1: CIS PROLINE - PRO 30 / 2: CIS PROLINE - PRO 202 |
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Components
#1: Protein | ![]() Mass: 29100.812 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-HG / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.05 % | ||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 20 ℃ / pH: 8 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 25, 1993 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Num. obs: 19242 / % possible obs: 79 % / Observed criterion σ(I): 2 / Redundancy: 2.2 % / Rmerge(I) obs: 0.1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 8 Å / Num. measured all: 42585 / Rmerge(I) obs: 0.1 |
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Processing
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Refinement | Resolution: 1.8→8 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 16.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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