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- PDB-2cab: STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cab | |||||||||
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Title | STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I | |||||||||
![]() | CARBONIC ANHYDRASE FORM B | |||||||||
![]() | HYDRO-LYASE | |||||||||
Function / homology | ![]() 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 / zinc ion binding / extracellular exosome / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Kannan, K.K. / Ramanadham, M. / Jones, T.A. | |||||||||
![]() | ![]() Title: Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I Authors: Kannan, K.K. / Ramanadham, M. / Jones, T.A. #1: ![]() Year: 1980 Title: Structure and Function of Carbonic Anhydrases Authors: Kannan, K.K. #2: ![]() Title: Crystal Structure of Carbonic Anhydrase Authors: Kannan, K.K. #3: ![]() Title: Structure, Refinement, and Function of Human Carbonic Anhydrase-B Authors: Kannan, K.K. / Ramanadham, M. #4: ![]() Title: Structure and Function of Carbonic Anhydrases. Imidazole Binding to Human Carbonic Anhydrace B and the Mechanism of Action of Carbonic Anhydrases Authors: Kannan, K.K. / Petef, M. / Fridborg, K. / Cid-Dresdner, H. / Lovgren, S. #5: ![]() Title: Crystal Structure of Human Erythrocyte Carbonic Anhydrase B, Three-Dimensional Structure at a Nominal 2.2 Angstroms Resolution Authors: Kannan, K.K. / Notstrand, B. / Fridborg, K. / Lovgren, S. / Ohlsson, A. / Petef, M. #6: ![]() Title: Structural Relationship of Human Erythrocyte Carbonic Anhydrase Isozymes B and C Authors: Notstrand, B. / Vaara, I. / Kannan, K.K. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 62.7 KB | Display | ![]() |
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PDB format | ![]() | 44.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 372.8 KB | Display | ![]() |
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Full document | ![]() | 389.7 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 30 AND 202 ARE CIS-PROLINES. / 2: CYSTINE 212 IS MODIFIABLE BY MERCURIALS. / 3: HISTIDINE RESIDUES 94, 96 AND 119 ARE ZINC LIGANDS. 4: HISTIDINE RESIDUES 64, 67 AND 200 ARE IN THE ACTIVE SITE. 5: SEE REMARK 7. |
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Components
#1: Protein | Mass: 28789.016 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-ZN / |
Sequence details | RESIDUE 74 IN THIS ENTRY IS IDENTIFIED AS GLN. HOWEVER, CHEMICAL SEQUENCE AND RECENT DIFFRACTION ...RESIDUE 74 IN THIS ENTRY IS IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.26 % |
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Processing
Software | Name: CORELS / Classification: refinement | ||||||||||||
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Refinement | Rfactor Rwork: 0.193 / Highest resolution: 2 Å Details: HELICES E1 AND E2 WERE ASSIGNED DEFAULT TYPE 1 (ALPHA). | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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