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- PDB-3t5u: Crystal structure of the human carbonic anhydrase II in complex w... -

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Basic information

Entry
Database: PDB / ID: 3t5u
TitleCrystal structure of the human carbonic anhydrase II in complex with N-hydroxy benzenesulfonamide
ComponentsCarbonic anhydrase 2
KeywordsLYASE/LYASE INHIBITOR / Protein-inhibitor complex / LYASE-LYASE INHIBITOR complex
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 / angiotensin-activated signaling pathway / regulation of chloride transport / 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 / angiotensin-activated signaling pathway / regulation of chloride transport / Reversible hydration of carbon dioxide / regulation of intracellular pH / positive regulation of synaptic transmission, GABAergic / 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 / 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
N-hydroxybenzenesulfonamide / MERCURIBENZOIC ACID / Carbonic anhydrase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.75 Å
AuthorsDi Fiore, A. / Maresca, A. / Alterio, V. / Supuran, C.T. / De Simone, G.
Citation
Journal: Chem.Commun.(Camb.) / Year: 2011
Title: Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II.
Authors: Di Fiore, A. / Maresca, A. / Alterio, V. / Supuran, C.T. / De Simone, G.
#1: Journal: Proteins / Year: 1988
Title: Refined structure of human carbonic anhydrase II at 2.0 A resolution.
Authors: Eriksson, A.E. / Jones, T.A. / Liljas, A.
#2: Journal: Chemmedchem / Year: 2009
Title: Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitors.
Authors: Scott, A.D. / Phillips, C. / Alex, A. / Flocco, M. / Bent, A. / Randall, A. / O'Brien, R. / Damian, L. / Jones, L.H.
History
DepositionJul 28, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 20, 2012Provider: repository / Type: Initial release

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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)30,3308
Polymers29,1581
Non-polymers1,1727
Water4,774265
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)42.26, 41.54, 72.09
Angle α, β, γ (deg.)90.00, 104.43, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 1 molecules A

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


Mass: 29157.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P00918, carbonic anhydrase

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Non-polymers , 5 types, 272 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-A09 / N-hydroxybenzenesulfonamide / Piloty's acid


Mass: 173.190 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H7NO3S
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-MBO / MERCURIBENZOIC ACID


Mass: 321.703 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H5HgO2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 265 / 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: 2.1 Å3/Da / Density % sol: 41.47 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 2.6 M ammonium sulfate, 0.3 M sodium chloride, 0.1 M Tris-HCl, pH 8.5, 5 mM 4-hydroxymercurybenzoate, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å
DetectorType: RIGAKU SATURN / Detector: CCD / Date: Feb 7, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.75→20 Å / Num. all: 24290 / Num. obs: 24290 / % possible obs: 98.2 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 21.38
Reflection shellResolution: 1.75→1.81 Å / Rmerge(I) obs: 0.097 / Mean I/σ(I) obs: 10.92 / Num. unique all: 2238 / % possible all: 91.2

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Processing

Software
NameClassification
CrystalCleardata collection
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB ENTRY 1CA2

1ca2


Resolution: 1.75→20 Å / Occupancy max: 1 / Occupancy min: 0.5 / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.1827 1162 4.7 %RANDOM
Rwork0.171 22913 --
all-24290 --
obs-24075 97.5 %-
Solvent computationBsol: 48.709 Å2
Displacement parametersBiso max: 46.27 Å2 / Biso mean: 15.4145 Å2 / Biso min: 3.19 Å2
Baniso -1Baniso -2Baniso -3
1--0.237 Å20 Å21.139 Å2
2---3.444 Å20 Å2
3---3.681 Å2
Refinement stepCycle: LAST / Resolution: 1.75→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2040 0 61 265 2366
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_mcbond_it1.0941.5
X-RAY DIFFRACTIONc_scbond_it1.842
X-RAY DIFFRACTIONc_mcangle_it1.6212
X-RAY DIFFRACTIONc_scangle_it2.7822.5
Xplor file
Refine-IDSerial noParam file
X-RAY DIFFRACTION1protein_rep.param
X-RAY DIFFRACTION2CNS_TOPPAR:ion.param
X-RAY DIFFRACTION3CNS_TOPPAR:water_rep.param
X-RAY DIFFRACTION4gol.par
X-RAY DIFFRACTION5a09.par

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