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- PDB-5gxo: Discovery of a compound that activates SIRT3 to deacetylate Manga... -

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Basic information

Entry
Database: PDB / ID: 5gxo
TitleDiscovery of a compound that activates SIRT3 to deacetylate Manganese Superoxide Dismutase
ComponentsSuperoxide dismutase [Mn], mitochondrial
KeywordsOXIDOREDUCTASE / superoxide dismutase acetylation
Function / homology
Function and homology information


acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure / negative regulation of membrane hyperpolarization / : / positive regulation of hydrogen peroxide biosynthetic process / response to magnetism / response to silicon dioxide / response to selenium ion / response to L-ascorbic acid / intracellular oxygen homeostasis / response to superoxide ...acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure / negative regulation of membrane hyperpolarization / : / positive regulation of hydrogen peroxide biosynthetic process / response to magnetism / response to silicon dioxide / response to selenium ion / response to L-ascorbic acid / intracellular oxygen homeostasis / response to superoxide / response to manganese ion / hydrogen peroxide biosynthetic process / response to zinc ion / superoxide metabolic process / positive regulation of vascular associated smooth muscle cell apoptotic process / superoxide dismutase / Detoxification of Reactive Oxygen Species / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / superoxide dismutase activity / response to isolation stress / response to immobilization stress / negative regulation of vascular associated smooth muscle cell proliferation / mitochondrial nucleoid / response to electrical stimulus / cellular response to ethanol / response to cadmium ion / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / Mitochondrial unfolded protein response (UPRmt) / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / removal of superoxide radicals / release of cytochrome c from mitochondria / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / response to activity / response to hydrogen peroxide / Transcriptional activation of mitochondrial biogenesis / oxygen binding / regulation of blood pressure / manganese ion binding / response to lipopolysaccharide / cellular response to oxidative stress / negative regulation of neuron apoptotic process / protein homotetramerization / response to hypoxia / response to xenobiotic stimulus / positive regulation of cell migration / mitochondrial matrix / negative regulation of cell population proliferation / regulation of transcription by RNA polymerase II / enzyme binding / mitochondrion / DNA binding / extracellular exosome / identical protein binding
Similarity search - Function
: / Iron/manganese superoxide dismutase, C-terminal domain / Fe,Mn superoxide dismutase (SOD) domain / minor pseudopilin epsh fold / 3-Layer(bab) Sandwich / Manganese/iron superoxide dismutase, binding site / Manganese and iron superoxide dismutases signature. / Manganese/iron superoxide dismutase / Manganese/iron superoxide dismutase, N-terminal / Iron/manganese superoxide dismutases, alpha-hairpin domain ...: / Iron/manganese superoxide dismutase, C-terminal domain / Fe,Mn superoxide dismutase (SOD) domain / minor pseudopilin epsh fold / 3-Layer(bab) Sandwich / Manganese/iron superoxide dismutase, binding site / Manganese and iron superoxide dismutases signature. / Manganese/iron superoxide dismutase / Manganese/iron superoxide dismutase, N-terminal / Iron/manganese superoxide dismutases, alpha-hairpin domain / Manganese/iron superoxide dismutase, C-terminal / Manganese/iron superoxide dismutase, C-terminal domain superfamily / Manganese/iron superoxide dismutase, N-terminal domain superfamily / Iron/manganese superoxide dismutases, C-terminal domain / Helix Hairpins / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / Superoxide dismutase [Mn], mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsLu, J. / Li, J. / Wu, M. / Wang, J. / Xia, Q.
Funding support China, 1items
OrganizationGrant numberCountry
China
CitationJournal: Free Radic. Biol. Med. / Year: 2017
Title: A small molecule activator of SIRT3 promotes deacetylation and activation of manganese superoxide dismutase.
Authors: Lu, J. / Zhang, H. / Chen, X. / Zou, Y. / Li, J. / Wang, L. / Wu, M. / Zang, J. / Yu, Y. / Zhuang, W. / Xia, Q. / Wang, J.
History
DepositionSep 19, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 9, 2017Provider: repository / Type: Initial release
Revision 1.1Dec 6, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2Nov 8, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model / struct_conn / struct_conn_type
Item: _citation.country / _database_2.pdbx_DOI ..._citation.country / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_conn_type.id
Revision 1.3Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Superoxide dismutase [Mn], mitochondrial
B: Superoxide dismutase [Mn], mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,6584
Polymers44,5482
Non-polymers1102
Water2,540141
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Superoxide dismutase [Mn], mitochondrial
B: Superoxide dismutase [Mn], mitochondrial
hetero molecules

A: Superoxide dismutase [Mn], mitochondrial
B: Superoxide dismutase [Mn], mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,3168
Polymers89,0974
Non-polymers2204
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation12_545x,x-y-1,-z+1/61
Buried area8130 Å2
ΔGint-44 kcal/mol
Surface area31280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)80.120, 80.120, 242.870
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein Superoxide dismutase [Mn], mitochondrial


Mass: 22274.141 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SOD2 / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: P04179, superoxide dismutase
#2: Chemical ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: Mn
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 141 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.54 Å3/Da / Density % sol: 51.58 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 1.5M potassium phosphate pH 7.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9791 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 24, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.3→52.74 Å / Num. obs: 21413 / % possible obs: 99.6 % / Redundancy: 16.1 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 17.8
Reflection shellResolution: 2.3→2.42 Å / Redundancy: 17.4 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 10.9 / % possible all: 100

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Processing

Software
NameVersionClassification
iMOSFLMdata processing
SCALAdata scaling
PHASERphasing
Cootmodel building
REFMAC5.7.0032refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1SZX

1szx


Resolution: 2.3→52.74 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.907 / SU B: 7.338 / SU ML: 0.174 / Cross valid method: THROUGHOUT / ESU R: 0.332 / ESU R Free: 0.234 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24975 1095 5.1 %RANDOM
Rwork0.21308 ---
obs0.21498 20241 99.48 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 31.362 Å2
Baniso -1Baniso -2Baniso -3
1-0.07 Å20.07 Å20 Å2
2--0.07 Å20 Å2
3----0.23 Å2
Refinement stepCycle: 1 / Resolution: 2.3→52.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3090 0 2 141 3233
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.0193182
X-RAY DIFFRACTIONr_bond_other_d0.0050.022945
X-RAY DIFFRACTIONr_angle_refined_deg1.2971.934331
X-RAY DIFFRACTIONr_angle_other_deg0.86636755
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.2965392
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.85424.834151
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.29915480
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.227158
X-RAY DIFFRACTIONr_chiral_restr0.0830.2450
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0213700
X-RAY DIFFRACTIONr_gen_planes_other0.0070.02784
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.3043.0091574
X-RAY DIFFRACTIONr_mcbond_other2.2983.0081573
X-RAY DIFFRACTIONr_mcangle_it3.2664.5071964
X-RAY DIFFRACTIONr_mcangle_other3.2664.5081965
X-RAY DIFFRACTIONr_scbond_it2.9453.2241608
X-RAY DIFFRACTIONr_scbond_other2.9443.2251609
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.4534.7142368
X-RAY DIFFRACTIONr_long_range_B_refined6.0128.45813586
X-RAY DIFFRACTIONr_long_range_B_other6.00828.43613516
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.329 69 -
Rwork0.3 1481 -
obs--100 %

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