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- PDB-7d8g: The crystal structure of nucleotide phosphatase Sa1684 from Staph... -

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Basic information

Entry
Database: PDB / ID: 7d8g
TitleThe crystal structure of nucleotide phosphatase Sa1684 from Staphylococcus aureus
ComponentsUPF0374 protein SA1684
KeywordsCYTOSOLIC PROTEIN / nucleotide phospatase
Function / homology
Function and homology information


nucleoside diphosphate phosphatase / nucleoside diphosphate phosphatase activity / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / magnesium ion binding
Similarity search - Function
Uncharacterised protein family UPF0374 / FomD barrel-like fold / FomD-like / : / Domain of unknown function DUF402 / FomD-like superfamily / Protein of unknown function (DUF402) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
CITRIC ACID / Nucleoside triphosphate/diphosphate phosphatase
Similarity search - Component
Biological speciesStaphylococcus aureus subsp. aureus N315 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.5 Å
AuthorsWang, Z. / Li, X.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971124 China
Citation
Journal: Febs J. / Year: 2021
Title: The structural mechanism for the nucleoside tri- and diphosphate hydrolysis activity of Ntdp from Staphylococcus aureus.
Authors: Wang, Z. / Shen, H. / He, B. / Teng, M. / Guo, Q. / Li, X.
#1: Journal: J. Biol. Chem. / Year: 2016
Title: Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence
Authors: Kenta, I. / Yuki, S.
History
DepositionOct 8, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 17, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 6, 2021Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Feb 16, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.3Jun 7, 2023Group: Data collection / Category: diffrn_source / Item: _diffrn_source.source
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: UPF0374 protein SA1684
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,1606
Polymers21,7351
Non-polymers4255
Water1,928107
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: native gel electrophoresis
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area170 Å2
ΔGint-15 kcal/mol
Surface area9340 Å2
MethodPISA
Unit cell
Length a, b, c (Å)48.906, 36.056, 56.309
Angle α, β, γ (deg.)90.000, 109.160, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein UPF0374 protein SA1684


Mass: 21734.592 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus subsp. aureus N315 (bacteria)
Strain: N315 / Gene: SA1684 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q7A4T2
#2: Chemical ChemComp-CIT / CITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7 / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 107 / 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: 2.2 Å3/Da / Density % sol: 44.08 %
Crystal growTemperature: 289.15 K / Method: vapor diffusion, hanging drop / Details: 20% PEG400, 0.1M sodium citrate pH 5.5.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.98752 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jan 18, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98752 Å / Relative weight: 1
ReflectionResolution: 1.5→50 Å / Num. obs: 29587 / % possible obs: 98.6 % / Redundancy: 6.7 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 27.25
Reflection shellResolution: 1.5→1.53 Å / Num. unique obs: 1466 / CC1/2: 0.968 / % possible all: 95.3

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Processing

Software
NameVersionClassification
REFMAC5.8.0258refinement
HKL-2000data scaling
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 1.5→30.32 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.959 / SU B: 1.199 / SU ML: 0.045 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.069 / ESU R Free: 0.069 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.1887 1429 4.8 %RANDOM
Rwork0.1654 ---
obs0.1664 28146 98.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 52.17 Å2 / Biso mean: 14.504 Å2 / Biso min: 5.62 Å2
Baniso -1Baniso -2Baniso -3
1-0.06 Å2-0 Å2-0.83 Å2
2---0.55 Å2-0 Å2
3---0.86 Å2
Refinement stepCycle: final / Resolution: 1.5→30.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1477 0 27 107 1611
Biso mean--25.29 24.29 -
Num. residues----174
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0131546
X-RAY DIFFRACTIONr_bond_other_d0.0020.0171373
X-RAY DIFFRACTIONr_angle_refined_deg1.791.6442093
X-RAY DIFFRACTIONr_angle_other_deg1.4881.5843198
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.2055175
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.38222.96791
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.41315268
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.659158
X-RAY DIFFRACTIONr_chiral_restr0.090.2192
X-RAY DIFFRACTIONr_gen_planes_refined0.010.021701
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02335
LS refinement shellResolution: 1.501→1.54 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.234 104 -
Rwork0.195 2010 -
all-2114 -
obs--97.33 %

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