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- PDB-6got: Crystal structure of human carbonic anhydrase II in complex with ... -

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Basic information

Entry
Database: PDB / ID: 6got
TitleCrystal structure of human carbonic anhydrase II in complex with the inhibitor 4-(phenethylthio)benzenesulfonamide
ComponentsCarbonic anhydrase 2
KeywordsLYASE
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 / angiotensin-activated signaling pathway / Reversible hydration of carbon dioxide ...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 / angiotensin-activated signaling pathway / Reversible hydration of carbon dioxide / regulation of intracellular pH / positive regulation of synaptic transmission, GABAergic / hydro-lyase activity / 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 / apical part of cell / one-carbon metabolic process / myelin sheath / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase ...Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase / Roll / Alpha Beta
Similarity search - Domain/homology
4-(2-phenylethylsulfanyl)benzenesulfonamide / Carbonic anhydrase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.56 Å
AuthorsFerraroni, M. / Supuran, C.T. / Angeli, A.
CitationJournal: Bioorg. Chem. / Year: 2018
Title: Synthesis of different thio-scaffolds bearing sulfonamide with subnanomolar carbonic anhydrase II and IX inhibitory properties and X-ray investigations for their inhibitory mechanism.
Authors: Angeli, A. / Tanini, D. / Capperucci, A. / Malevolti, G. / Turco, F. / Ferraroni, M. / Supuran, C.T.
History
DepositionJun 4, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 3, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 10, 2018Group: Data collection / Structure summary / Category: entity / Item: _entity.formula_weight

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Carbonic anhydrase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7895
Polymers29,2461
Non-polymers5434
Water2,234124
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area430 Å2
ΔGint-1 kcal/mol
Surface area11490 Å2
MethodPISA
Unit cell
Length a, b, c (Å)42.443, 41.284, 72.171
Angle α, β, γ (deg.)90.000, 104.380, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Carbonic anhydrase 2 / / Carbonate dehydratase II / Carbonic anhydrase C / CAC / Carbonic anhydrase II / CA-II


Mass: 29245.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: erytrocytes / Source: (natural) Homo sapiens (human) / References: UniProt: P00918, carbonic anhydrase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-F6W / 4-(2-phenylethylsulfanyl)benzenesulfonamide


Mass: 293.404 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H15NO2S2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 124 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.09 Å3/Da / Density % sol: 41.18 %
Crystal growTemperature: 296 K / Method: vapor diffusion / pH: 8 / Details: 1.5 M sodium citrate, Tris 100 mM

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.827 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Mar 13, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.827 Å / Relative weight: 1
ReflectionResolution: 1.56→41.11 Å / Num. obs: 33578 / % possible obs: 96.5 % / Redundancy: 4.21 % / CC1/2: 0.99 / Rmerge(I) obs: 0.173 / Rrim(I) all: 0.196 / Net I/σ(I): 5.48
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
1.56-1.674.270.81.2661310.5360.8896.1
1.67-1.84.270.6031.8954880.6940.63696.6
1.8-1.974.250.3953.1251510.8490.39496.2
1.97-2.24.170.264.7646510.9230.25496
2.54-3.114.240.0139.2736010.980.12697.4
3.11-4.393.940.07514.1328300.9920.07798.6
4.39-41.114.190.06416.8415830.9960.06696.6

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
REFMACrefinement
PDB_EXTRACT3.24data extraction
REFMACphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4FIK

4fik


Resolution: 1.56→41.11 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.935 / SU B: 2.393 / SU ML: 0.083 / SU R Cruickshank DPI: 0.0992 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.099 / ESU R Free: 0.094 / Details: U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2233 1679 5 %RANDOM
Rwork0.1988 ---
obs0.2001 31883 96.51 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 68.05 Å2 / Biso mean: 15.776 Å2 / Biso min: 7.33 Å2
Baniso -1Baniso -2Baniso -3
1--0.2 Å20 Å2-0.01 Å2
2--0.28 Å20 Å2
3----0.06 Å2
Refinement stepCycle: final / Resolution: 1.56→41.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2044 0 32 124 2200
Biso mean--31.1 21.22 -
Num. residues----257
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0192150
X-RAY DIFFRACTIONr_angle_refined_deg1.711.9632915
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.1415261
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.73524.74297
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.6915358
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.266157
X-RAY DIFFRACTIONr_chiral_restr0.1180.2306
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0211636
LS refinement shellResolution: 1.56→1.601 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.314 121 -
Rwork0.291 2362 -
all-2483 -
obs--96.02 %

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