+Open data
-Basic information
Entry | Database: PDB / ID: 1crm | ||||||
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Title | STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES | ||||||
Components | CARBONIC ANHYDRASE I | ||||||
Keywords | LYASE (OXO-ACID) | ||||||
Function / homology | Function and homology information hydro-lyase activity / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / Reversible hydration of carbon dioxide / carbonic anhydrase / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen ...hydro-lyase activity / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / Reversible hydration of carbon dioxide / carbonic anhydrase / carbonate dehydratase activity / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / one-carbon metabolic process / extracellular exosome / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Yadava, V.S. / Kannan, K.K. | ||||||
Citation | Journal: Biomolecular Structure, Conformation, Function and Evolution Year: 1981 Title: Structure and Function of Carbonic Anhydrases Authors: Kannan, K.K. #1: Journal: J.Mol.Biol. / Year: 1972 Title: Structure of Human Carbonic Anhydrase B. I. Crystallization and Heavy Atom Modification Authors: Kannan, K.K. / Fridborg, K. / Bergsten, P.C. / Liljas, A. / Lovgren, S. / Petef, M. / Strandberg, B. / Waara, I. / Alder, L. / Falkbring, S.O. / Gothe, P.O. / Nyman, P.O. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE ...SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. STRANDS 1 - 3 AND 5 - 10 OF AS1 AND BS1 ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1crm.cif.gz | 69.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1crm.ent.gz | 51.6 KB | Display | PDB format |
PDBx/mmJSON format | 1crm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cr/1crm ftp://data.pdbj.org/pub/pdb/validation_reports/cr/1crm | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 30 / 2: CIS PROLINE - PRO 202 |
-Components
#1: Protein | Mass: 28789.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P00915, carbonic anhydrase | ||||||||||
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#2: Chemical | ChemComp-HG / #3: Chemical | #4: Chemical | ChemComp-H2S / | #5: Water | ChemComp-HOH / | Compound details | SECONDARY STRUCTURE ELEMENTS AND TURNS HAVE BEEN IDENTIFIED USING W.KABSCH AND C.SANDER'S ALGORITHM ...SECONDARY STRUCTURE ELEMENTS AND TURNS HAVE BEEN IDENTIFIED | Nonpolymer details | THE HG2+ WHICH REPLACES ZN2+ IS 0.5A AWAY FROM ZN2+ POSITION IN THE NATIVE ENZYME. RESIDUES SER 188 ...THE HG2+ WHICH REPLACES ZN2+ IS 0.5A AWAY FROM ZN2+ POSITION IN THE NATIVE ENZYME. RESIDUES SER 188 AND LEU 189 HAVE MOVED BY LARGE DISTANCE COMPARED TO THE NATIVE STRUCTURE. THE WATER MOLECULE OBSERVED AT FOURTH COORDINATI | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.11 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Resolution: 2→8 Å / σ(F): 2 Details: THE HG2+ BOUND TO CYS 212 IS DISORDERED WITH TWO SITES FOR HG2+ SEPARATED BY ABOUT 1.6 ANGSTROMS. CYS 212 SHOWS MULTIPLE CONFORMATIONS. THESE FEATURES ARE CLEARLY SEEN IN (FO - FC) MAP.
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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