[English] 日本語
Yorodumi- PDB-1bcd: X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1bcd | ||||||
---|---|---|---|---|---|---|---|
Title | X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE | ||||||
Components | CARBONIC ANHYDRASE IICarbonic anhydrase | ||||||
Keywords | LYASE(OXO-ACID) | ||||||
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 / regulation of intracellular pH / morphogenesis of an epithelium / 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 / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Hakansson, K. / Liljas, A. | ||||||
Citation | Journal: FEBS Lett. / Year: 1994 Title: The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide. Authors: Hakansson, K. / Liljas, A. #1: Journal: Int.J.Biol.Macromol. / Year: 1993 Title: Refined Structure of the Aminobenzolamide Complex of Human Carbonic Anhydrase II at 1.9 Angstroms Authors: Vidgren, J. / Svensson, A. / Liljas, A. #2: Journal: J.Mol.Biol. / Year: 1992 Title: Structure of Native and Apo Carbonic Anhydrase II and Structure of Some of its Anion-Ligand Complexes Authors: Hakansson, K. / Carlsson, M. / Svensson, L.A. / Liljas, A. #3: Journal: J.Mol.Biol. / Year: 1992 Title: Structure of Cobalt Carbonic Anhydrase Complexed with Bicarbonate Authors: Hakansson, K. / Wehnert, A. #4: Journal: Int.J.Biol.Macromol. / Year: 1990 Title: Refined Structure of the Acetazolamide Complex of Human Carbonic Anhydrase II at 1.9 Angstroms Authors: Vidgren, J. / Liljas, A. / Walker, N.P.C. | ||||||
History |
| ||||||
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. RESIDUES 4, 14, 64 AND 136 ARE PRESENTED WITH TWO ALTERNATIVE CONFORMATIONS. RESIDUE 3 HAS PARTIAL OCCUPANCY. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1bcd.cif.gz | 70.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1bcd.ent.gz | 51 KB | Display | PDB format |
PDBx/mmJSON format | 1bcd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bc/1bcd ftp://data.pdbj.org/pub/pdb/validation_reports/bc/1bcd | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO 30 / 2: CIS PROLINE - PRO 202 |
-Components
#1: Protein | Mass: 29157.863 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P00918, carbonic anhydrase |
---|---|
#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-FMS / |
#4: Water | ChemComp-HOH / |
Sequence details | RESIDUES 125 AND 127 ARE ADJACENT IN THE SEQUENCE. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.89 % | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Method: other | ||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 1.93 Å / Lowest resolution: 3.5 Å / Num. all: 19036 / Num. obs: 16783 / % possible obs: 88.2 % / Num. measured all: 46466 / Rmerge(I) obs: 0.083 |
---|
-Processing
Software | Name: PROFFT / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor obs: 0.154 / Highest resolution: 1.9 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.93 Å / Rfactor obs: 0.154 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 13.3 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|