+Open data
-Basic information
Entry | Database: PDB / ID: 1znc | ||||||
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Title | HUMAN CARBONIC ANHYDRASE IV | ||||||
Components | CARBONIC ANHYDRASE IV | ||||||
Keywords | LYASE / GPI-ANCHOR / MEMBRANE / ZINC | ||||||
Function / homology | Function and homology information bicarbonate transport / transport vesicle membrane / endoplasmic reticulum-Golgi intermediate compartment / rough endoplasmic reticulum / secretory granule membrane / Reversible hydration of carbon dioxide / carbonic anhydrase / brush border membrane / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide ...bicarbonate transport / transport vesicle membrane / endoplasmic reticulum-Golgi intermediate compartment / rough endoplasmic reticulum / secretory granule membrane / Reversible hydration of carbon dioxide / carbonic anhydrase / brush border membrane / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / trans-Golgi network / one-carbon metabolic process / apical plasma membrane / external side of plasma membrane / perinuclear region of cytoplasm / Golgi apparatus / cell surface / zinc ion binding / extracellular exosome / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Stams, T. / Christianson, D.W. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 Title: Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution. Authors: Stams, T. / Nair, S.K. / Okuyama, T. / Waheed, A. / Sly, W.S. / Christianson, D.W. #1: Journal: Arch.Biochem.Biophys. / Year: 1996 Title: Carbonic Anhydrase Iv: Purification of a Secretory Form of the Recombinant Human Enzyme and Identification of the Positions and Importance of its Disulfide Bonds Authors: Waheed, A. / Okuyama, T. / Heyduk, T. / Sly, W.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1znc.cif.gz | 131.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1znc.ent.gz | 102.9 KB | Display | PDB format |
PDBx/mmJSON format | 1znc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1znc_validation.pdf.gz | 385.2 KB | Display | wwPDB validaton report |
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Full document | 1znc_full_validation.pdf.gz | 390.9 KB | Display | |
Data in XML | 1znc_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 1znc_validation.cif.gz | 17.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zn/1znc ftp://data.pdbj.org/pub/pdb/validation_reports/zn/1znc | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 30364.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HUMAN CAIV / Plasmid: PCAGGS / Cell line (production host): CHO-CELLS / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P22748, carbonic anhydrase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | THE RESIDUE NUMBERING IS BASED ON THE RESIDUE NUMBERING OF CARBONIC ANHYDRASE II. INSERTIONS ARE ...THE RESIDUE NUMBERING IS BASED ON THE RESIDUE NUMBERING OF CARBONIC ANHYDRASE II. INSERTIONS | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.9 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.1 / Details: 25% PEG 3,350; 100MM NA ACETATE PH 5.1 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 13626 / % possible obs: 95 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.08 |
Reflection shell | Resolution: 2.8→2.87 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.253 / % possible all: 91.8 |
Reflection | *PLUS Num. measured all: 46250 |
Reflection shell | *PLUS % possible obs: 91.8 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: POLYALANINE MODEL OF CAII MISSING N-TERMINAL 30 Resolution: 2.8→20 Å / Cross valid method: FREE-R / σ(F): 2
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Displacement parameters | Biso mean: 28.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | Rms dev position: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.8→2.93 Å
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.28 |