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- PDB-1v79: Crystal structures of adenosine deaminase complexed with potent i... -

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Basic information

Entry
Database: PDB / ID: 1v79
TitleCrystal structures of adenosine deaminase complexed with potent inhibitors
ComponentsAdenosine deaminase
KeywordsHYDROLASE / beta barrel / zinc
Function / homology
Function and homology information


negative regulation of adenosine receptor signaling pathway / cytoplasmic vesicle lumen / inosine biosynthetic process / adenosine deaminase / 2'-deoxyadenosine deaminase activity / hypoxanthine salvage / adenosine catabolic process / purine ribonucleoside monophosphate biosynthetic process / adenosine deaminase activity / nucleotide metabolic process ...negative regulation of adenosine receptor signaling pathway / cytoplasmic vesicle lumen / inosine biosynthetic process / adenosine deaminase / 2'-deoxyadenosine deaminase activity / hypoxanthine salvage / adenosine catabolic process / purine ribonucleoside monophosphate biosynthetic process / adenosine deaminase activity / nucleotide metabolic process / anchoring junction / T cell activation / lysosome / cell adhesion / external side of plasma membrane / zinc ion binding / cytosol
Similarity search - Function
Adenosine deaminase / Adenosine/AMP deaminase active site / Adenosine and AMP deaminase signature. / Adenosine deaminase domain / Adenosine deaminase / Adenosine/adenine deaminase / Metal-dependent hydrolases / Metal-dependent hydrolase / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Chem-FR7 / Adenosine deaminase
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsKinoshita, T.
CitationJournal: J.Med.Chem. / Year: 2004
Title: Structure-based design and synthesis of non-nucleoside, potent, and orally bioavailable adenosine deaminase inhibitors
Authors: Terasaka, T. / Okumura, H. / Tsuji, K. / Kato, T. / Nakanishi, I. / Kinoshita, T. / Kato, Y. / Kuno, M. / Seki, N. / Naoe, Y. / Inoue, T. / Tanaka, K. / Nakamura, K.
History
DepositionDec 14, 2003Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 21, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Adenosine deaminase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)40,7493
Polymers40,3421
Non-polymers4082
Water2,630146
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)77.230, 77.230, 135.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein Adenosine deaminase / Adenosine aminohydrolase


Mass: 40341.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P56658, adenosine deaminase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-FR7 / 1-{(1R,2S)-1-[2-(2,3,-DICHLOROPHENYL)ETHYL]-2-HYDROXYPROPYL}-1H-IMIDAZOLE-4-CARBOXAMIDE / FR239087


Mass: 342.220 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C15H17Cl2N3O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 146 / 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: 2.43 Å3/Da / Density % sol: 49.03 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6
Details: Ammonium sulphate, PEG400, MES buffer, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL24XU / Wavelength: 0.8266 Å
DetectorType: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Oct 25, 2003 / Details: graphite
RadiationMonochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.8266 Å / Relative weight: 1
ReflectionResolution: 2.5→12 Å / Num. all: 14623 / Num. obs: 13950 / % possible obs: 95.4 % / Observed criterion σ(I): 0

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Processing

Software
NameVersionClassification
crystalcleardata collection
crystalcleardata reduction
AMoREphasing
CNXrefinement
CrystalClear(MSC/RIGAKU)data reduction
CrystalClear(MSC/RIGAKU)data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→12 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.281 701 random
Rwork0.252 --
all0.262 14651 -
obs0.256 13950 -
Refinement stepCycle: LAST / Resolution: 2.5→12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2789 0 23 146 2958

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