+Open data
-Basic information
Entry | Database: PDB / ID: 1h4n | ||||||
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Title | H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS | ||||||
Components | CARBONIC ANHYDRASE II | ||||||
Keywords | LYASE / OXO-ACID / ACETYLATION | ||||||
Function / homology | Function and homology information positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway ...positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway / positive regulation of synaptic transmission, GABAergic / morphogenesis of an epithelium / regulation of intracellular pH / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / neuron cellular homeostasis / one-carbon metabolic process / apical part of cell / myelin sheath / zinc ion binding / extracellular exosome / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2 Å | ||||||
Authors | Lesburg, C.A. / Christianson, D.W. | ||||||
Citation | Journal: Biochemistry / Year: 1997 Title: Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity. Authors: Lesburg, C.A. / Huang, C. / Christianson, D.W. / Fierke, C.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h4n.cif.gz | 67.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h4n.ent.gz | 48.4 KB | Display | PDB format |
PDBx/mmJSON format | 1h4n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1h4n_validation.pdf.gz | 371.3 KB | Display | wwPDB validaton report |
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Full document | 1h4n_full_validation.pdf.gz | 371.8 KB | Display | |
Data in XML | 1h4n_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 1h4n_validation.cif.gz | 10 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h4/1h4n ftp://data.pdbj.org/pub/pdb/validation_reports/h4/1h4n | HTTPS FTP |
-Related structure data
Related structure data | 1h9nC 1h9qC 2h4nC 2cbaS S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 29133.820 Da / Num. of mol.: 1 / Mutation: H94N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Description: THIS CAII VARIANT WAS PRODUCED USING OLIGONUCLEOTIDE-DIRECTED MUTAGENESIS OF THE CLONED HUMAN CAII GENE IN BL21 (DE3) PCAM Cell line: BL21 / Gene: CAII / Plasmid: BL21 / Gene (production host): CAII / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) PCAM / References: UniProt: P00918, carbonic anhydrase |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-TRS / |
#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: 2.17 Å3/Da / Density % sol: 43 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 Details: 2M (NH4)2SO4; 100 MM TRIS PH 8.0; 5 MM N-HEXYL BETA-D-GLUCOPYRANOSIDE | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 1, 1997 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 16217 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Biso Wilson estimate: 15.8 Å2 / Rmerge(I) obs: 0.067 / Rsym value: 0.067 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.223 / Mean I/σ(I) obs: 3.2 / Rsym value: 0.223 / % possible all: 70 |
Reflection | *PLUS Num. measured all: 45669 |
Reflection shell | *PLUS % possible obs: 70 % |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 2CBA LESS MUTANT SIDE CHAIN AND SOLVENT MOLECULES Resolution: 2→20 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 17.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Rfactor Rfree error: 0.031 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1F / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.219 |