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- PDB-1azm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1azm | ||||||
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Title | DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I | ||||||
![]() | CARBONIC ANHYDRASE I | ||||||
![]() | LYASE(OXO-ACID) / PROTEIN-DRUG INTERACTIONS / OXO-ACID LYASE / SULFONAMIDES | ||||||
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 / extracellular exosome / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Chakravarty, S. / Kannan, K.K. | ||||||
![]() | ![]() Title: Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme. Authors: Chakravarty, S. / Kannan, K.K. #1: ![]() Title: Drug Protein Interaction at the Molecular Level: A Study of Sulphonamide Carbonic Anhydrase Complexes Authors: Chakravarty, S. / Yadava, V.S. / Kumar, V. / Kannan, K.K. #2: ![]() Title: Structure and Function of Carbonic Anhydrase: Comparative Studies of Sulphonamide Binding to Human Erythrocyte Carbonic Anhydrases B and C Authors: Kannan, K.K. / Vaara, I. / Notstrand, B. / Lovgren, S. / Borell, A. / Fridborg, K. / Petef, M. | ||||||
History |
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Remark 700 | SHEET SHEET B1 OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET ...SHEET SHEET B1 OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS *B1A* AND *B1B* ARE DEFINED. STRANDS 5, 6, 7, 8, 9, AND 10 OF B1A ARE IDENTICAL TO STRANDS 2, 3, 4, 5, 6, AND 7 OF B1B, RESPECTIVELY. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67.9 KB | Display | ![]() |
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PDB format | ![]() | 50.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: CIS PROLINE - PRO 30 / 2: CIS PROLINE - PRO 202 3: THE SULFONAMIDE DRUG 5-ACETAMIDO-1,3, 4-THIADIAZOLE-2-SULFONAMIDE HAS BEEN ASSIGNED THE THREE LETTER CODE AZM IN THE COORDINATE FILE. 4: THE DRUG MOLECULE HAS WELL DEFINED ELECTRON DENSITY IN THE ACTIVE SITE OF THE ENZYME. WHEN THE DRUG BINDS TO THE ENZYME, THE LOOP REGION COMPRISING OF RESIDUES LEU 198, THR 199 AND HIS 200 ...4: THE DRUG MOLECULE HAS WELL DEFINED ELECTRON DENSITY IN THE ACTIVE SITE OF THE ENZYME. WHEN THE DRUG BINDS TO THE ENZYME, THE LOOP REGION COMPRISING OF RESIDUES LEU 198, THR 199 AND HIS 200 UNDERGOES A SIGNIFICANT CHANGE AS COMPARED TO THE NATIVE STRUCTURE. 5: ACTIVE SITE HYDROGEN BONDED SOLVENT NETWORK INVOLVING HIS 67 AND HIS 200 IS POSSIBLY IMPORTANT FOR THE CATALYTIC ACTIVITY AND INHIBITION OF THIS ISOENZYME. 6: ZINC ZN(II) IS THE CATALYTICALLY ESSENTIALL ZINC ION. |
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Components
#1: Protein | Mass: 28774.988 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-AZM / |
#4: Water | ChemComp-HOH / |
Compound details | THE DRUG MOLECULE HAS WELL DEFINED ELECTRON DENSITY IN THE ACTIVE SITE OF THE ENZYME. WHEN THE DRUG ...THE DRUG MOLECULE HAS WELL DEFINED ELECTRON DENSITY IN THE ACTIVE SITE OF THE ENZYME. WHEN THE DRUG BINDS TO THE ENZYME, THE LOOP REGION COMPRISING |
Nonpolymer details | ZINC ZN(II) IS THE CATALYTICA |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.14 % |
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Crystal grow | *PLUS Method: unknown |
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Processing
Software | Name: PROTEIN / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.195 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |