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- PDB-7dcb: The structure of the Arabidopsis thaliana guanosine deaminase com... -

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Basic information

Entry
Database: PDB / ID: 7dcb
TitleThe structure of the Arabidopsis thaliana guanosine deaminase complexed with inosine
ComponentsGuanosine deaminase
KeywordsHYDROLASE / deamination / GSDA / purine metabolism
Function / homology
Function and homology information


guanosine deaminase / guanosine deaminase activity / purine nucleoside catabolic process / zinc ion binding / nucleus / cytoplasm
Similarity search - Function
Cytidine and deoxycytidylate deaminase zinc-binding region / Cytidine Deaminase, domain 2 / Cytidine Deaminase; domain 2 / APOBEC/CMP deaminase, zinc-binding / Cytidine and deoxycytidylate deaminases zinc-binding region signature. / Cytidine and deoxycytidylate deaminase domain / Cytidine and deoxycytidylate deaminases domain profile. / Cytidine deaminase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
INOSINE / Guanosine deaminase
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsXie, W. / Jia, Q. / Zeng, H.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31870782 China
CitationJournal: Int J Mol Sci / Year: 2022
Title: Substrate Specificity of GSDA Revealed by Cocrystal Structures and Binding Studies.
Authors: Jia, Q. / Zhang, J. / Zeng, H. / Tang, J. / Xiao, N. / Gao, S. / Li, H. / Xie, W.
History
DepositionOct 23, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 27, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 15, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Guanosine deaminase
D: Guanosine deaminase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)35,7136
Polymers35,0462
Non-polymers6674
Water2,378132
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: homology, PDBePISA
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4510 Å2
ΔGint-101 kcal/mol
Surface area12020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)117.980, 117.980, 37.736
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number169
Space group name H-MP61
Space group name HallP61
Symmetry operation#1: x,y,z
#2: x-y,x,z+1/6
#3: y,-x+y,z+5/6
#4: -y,x-y,z+1/3
#5: -x+y,-x,z+2/3
#6: -x,-y,z+1/2

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Components

#1: Protein Guanosine deaminase / tRNA-specific adenosine deaminase TAD4 / AtTAD4


Mass: 17523.016 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: GSDA, TAD4, At5g28050 / Production host: Escherichia coli (E. coli) / References: UniProt: Q94BU8, guanosine deaminase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-NOS / INOSINE


Mass: 268.226 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H12N4O5 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 132 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.16 Å3/Da / Density % sol: 43.14 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 1.2 M Na-citrate and 0.1 M HEPES (pH 7.5)

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Data collection

DiffractionMean temperature: 277 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NFPSS / Beamline: BL19U1 / Wavelength: 0.979 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Apr 17, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 20634 / % possible obs: 99.5 % / Redundancy: 18.6 % / Biso Wilson estimate: 28.86 Å2 / CC1/2: 0.967 / Rmerge(I) obs: 0.223 / Net I/σ(I): 19.2
Reflection shellResolution: 2→2.07 Å / Redundancy: 13.8 % / Rmerge(I) obs: 0.759 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 1963 / CC1/2: 0.895 / % possible all: 97.5

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7DBF

7dbf


Resolution: 2→34.06 Å / SU ML: 0.1943 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 22.5149 / Stereochemistry target values: CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1975 982 4.79 %
Rwork0.1648 19511 -
obs0.1663 20493 99.31 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 34.15 Å2
Refinement stepCycle: LAST / Resolution: 2→34.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2359 0 40 132 2531
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00412443
X-RAY DIFFRACTIONf_angle_d0.6813306
X-RAY DIFFRACTIONf_chiral_restr0.0456371
X-RAY DIFFRACTIONf_plane_restr0.0049428
X-RAY DIFFRACTIONf_dihedral_angle_d5.65831438
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.10.271150.222680X-RAY DIFFRACTION96.31
2.1-2.240.23181450.18132763X-RAY DIFFRACTION99.73
2.24-2.410.20361370.16482766X-RAY DIFFRACTION99.86
2.41-2.650.22271680.16642774X-RAY DIFFRACTION100
2.65-3.030.23241590.16922784X-RAY DIFFRACTION100
3.03-3.820.16171110.16272858X-RAY DIFFRACTION99.97
3.82-34.060.1751470.15222886X-RAY DIFFRACTION99.51

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