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Yorodumi- PDB-1qrl: A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qrl | ||||||
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Title | A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA | ||||||
Components | CARBONIC ANHYDRASE | ||||||
Keywords | LYASE / BETA-HELIX | ||||||
Function / homology | Function and homology information bicarbonate binding / sulfate binding / cobalt ion binding / carbonic anhydrase / carbonate dehydratase activity / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Methanosarcina thermophila (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / ISOMORPHOUS REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Iverson, T.M. / Alber, B.E. / Kisker, C. / Ferry, J.G. / Rees, D.C. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Authors: Iverson, T.M. / Alber, B.E. / Kisker, C. / Ferry, J.G. / Rees, D.C. #1: Journal: Embo J. / Year: 1996 Title: A Left-Handed Beta-Helix Revealed by the Crystal Structure of the Carbonic Anhydrase from Methanosarcina thermophila Authors: Kisker, C. / Schindelin, H. / Alber, B. / Ferry, J. / Rees, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qrl.cif.gz | 55.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qrl.ent.gz | 39.8 KB | Display | PDB format |
PDBx/mmJSON format | 1qrl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qr/1qrl ftp://data.pdbj.org/pub/pdb/validation_reports/qr/1qrl | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 23019.453 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina thermophila (archaea) / Production host: Escherichia coli (E. coli) / References: UniProt: P40881 |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-BCT / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.48 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.8 Details: PEG8000 ammonium sulfate, bicarbonate, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 6.2 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.08 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 3, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→20 Å / Num. all: 16254 / Num. obs: 15570 / % possible obs: 96.9 % / Observed criterion σ(F): 3 / Observed criterion σ(I): 3 / Redundancy: 3.4 % / Biso Wilson estimate: 21 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 16 |
Reflection shell | Resolution: 1.85→1.91 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.238 / % possible all: 82.3 |
Reflection | *PLUS Num. measured all: 55426 |
Reflection shell | *PLUS % possible obs: 82.3 % / Mean I/σ(I) obs: 4.3 |
-Processing
Software |
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Refinement | Method to determine structure: ISOMORPHOUS REPLACEMENT / Resolution: 1.85→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: refmac
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Refinement step | Cycle: LAST / Resolution: 1.85→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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