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- PDB-8iq0: Crystal structure of hydrogen sulfide-bound superoxide dismutase ... -

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Basic information

Entry
Database: PDB / ID: 8iq0
TitleCrystal structure of hydrogen sulfide-bound superoxide dismutase in oxidized state
ComponentsSuperoxide dismutase [Cu-Zn]
KeywordsOXIDOREDUCTASE / dimer
Function / homology
Function and homology information


neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / retina homeostasis / negative regulation of cholesterol biosynthetic process / hydrogen peroxide biosynthetic process / auditory receptor cell stereocilium organization / regulation of protein kinase activity ...neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / retina homeostasis / negative regulation of cholesterol biosynthetic process / hydrogen peroxide biosynthetic process / auditory receptor cell stereocilium organization / regulation of protein kinase activity / myeloid cell homeostasis / muscle cell cellular homeostasis / superoxide metabolic process / heart contraction / positive regulation of catalytic activity / superoxide dismutase / transmission of nerve impulse / superoxide dismutase activity / regulation of multicellular organism growth / response to axon injury / glutathione metabolic process / ovarian follicle development / embryo implantation / reactive oxygen species metabolic process / dendrite cytoplasm / removal of superoxide radicals / regulation of mitochondrial membrane potential / locomotory behavior / response to organic substance / positive regulation of cytokine production / sensory perception of sound / response to hydrogen peroxide / regulation of blood pressure / peroxisome / protein polyubiquitination / ubiquitin-protein transferase activity / response to heat / protein-folding chaperone binding / cytoplasmic vesicle / spermatogenesis / proteasome-mediated ubiquitin-dependent protein catabolic process / response to ethanol / intracellular iron ion homeostasis / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / copper ion binding / neuronal cell body / protein homodimerization activity / protein-containing complex / mitochondrion / zinc ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Copper/Zinc superoxide dismutase signature 1. / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Superoxide dismutase, copper/zinc binding domain / Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily
Similarity search - Domain/homology
COPPER (II) ION / HYDROSULFURIC ACID / Superoxide dismutase [Cu-Zn]
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.88 Å
AuthorsZhou, J.H. / Huang, W.X. / Cheng, R.X. / Zhang, P.J. / Zhu, Y.C.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32071446 China
CitationJournal: Cell Rep / Year: 2023
Title: Hydrogen sulfide functions as a micro-modulator bound at the copper active site of Cu/Zn-SOD to regulate the catalytic activity of the enzyme.
Authors: Wu, D.D. / Jin, S. / Cheng, R.X. / Cai, W.J. / Xue, W.L. / Zhang, Q.Q. / Yang, L.J. / Zhu, Q. / Li, M.Y. / Lin, G. / Wang, Y.Z. / Mu, X.P. / Wang, Y. / Zhang, I.Y. / Zhang, Q. / Chen, Y. / ...Authors: Wu, D.D. / Jin, S. / Cheng, R.X. / Cai, W.J. / Xue, W.L. / Zhang, Q.Q. / Yang, L.J. / Zhu, Q. / Li, M.Y. / Lin, G. / Wang, Y.Z. / Mu, X.P. / Wang, Y. / Zhang, I.Y. / Zhang, Q. / Chen, Y. / Cai, S.Y. / Tan, B. / Li, Y. / Chen, Y.Q. / Zhang, P.J. / Sun, C. / Yin, Y. / Wang, M.J. / Zhu, Y.Z. / Tao, B.B. / Zhou, J.H. / Huang, W.X. / Zhu, Y.C.
History
DepositionMar 15, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 6, 2023Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Superoxide dismutase [Cu-Zn]
B: Superoxide dismutase [Cu-Zn]
C: Superoxide dismutase [Cu-Zn]
D: Superoxide dismutase [Cu-Zn]
E: Superoxide dismutase [Cu-Zn]
F: Superoxide dismutase [Cu-Zn]
G: Superoxide dismutase [Cu-Zn]
H: Superoxide dismutase [Cu-Zn]
I: Superoxide dismutase [Cu-Zn]
J: Superoxide dismutase [Cu-Zn]
K: Superoxide dismutase [Cu-Zn]
L: Superoxide dismutase [Cu-Zn]
M: Superoxide dismutase [Cu-Zn]
N: Superoxide dismutase [Cu-Zn]
O: Superoxide dismutase [Cu-Zn]
P: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)251,84657
Polymers249,17316
Non-polymers2,67341
Water29,5991643
1
A: Superoxide dismutase [Cu-Zn]
B: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4056
Polymers31,1472
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Superoxide dismutase [Cu-Zn]
D: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4677
Polymers31,1472
Non-polymers3205
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Superoxide dismutase [Cu-Zn]
F: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,5938
Polymers31,1472
Non-polymers4466
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: Superoxide dismutase [Cu-Zn]
H: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4056
Polymers31,1472
Non-polymers2584
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
I: Superoxide dismutase [Cu-Zn]
J: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,5017
Polymers31,1472
Non-polymers3545
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
K: Superoxide dismutase [Cu-Zn]
L: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,5368
Polymers31,1472
Non-polymers3896
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
M: Superoxide dismutase [Cu-Zn]
N: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,5018
Polymers31,1472
Non-polymers3546
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
O: Superoxide dismutase [Cu-Zn]
P: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4407
Polymers31,1472
Non-polymers2935
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)74.348, 91.474, 91.164
Angle α, β, γ (deg.)85.000, 78.060, 66.760
Int Tables number1
Space group name H-MP1
Space group name HallP1
Symmetry operation#1: x,y,z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 1 through 14 or (resid 15...
d_2ens_1(chain "B" and (resid 1 through 8 or (resid 9...
d_3ens_1(chain "C" and (resid 1 through 8 or (resid 9...
d_4ens_1(chain "D" and (resid 1 through 8 or (resid 9...
d_5ens_1(chain "E" and (resid 1 through 8 or (resid 9...
d_6ens_1(chain "F" and (resid 1 through 8 or (resid 9...
d_7ens_1(chain "G" and (resid 1 through 8 or (resid 9...
d_8ens_1(chain "H" and (resid 1 through 8 or (resid 9...
d_9ens_1(chain "I" and (resid 1 through 8 or (resid 9...
d_10ens_1(chain "J" and (resid 1 through 8 or (resid 9...
d_11ens_1(chain "K" and (resid 1 through 8 or (resid 9...
d_12ens_1(chain "L" and (resid 1 through 8 or (resid 9...
d_13ens_1(chain "M" and (resid 1 through 8 or (resid 9...
d_14ens_1(chain "N" and (resid 1 through 8 or (resid 9...
d_15ens_1(chain "O" and (resid 1 through 14 or (resid 15...
d_16ens_1(chain "P" and (resid 1 through 8 or (resid 9...

NCS domain segments:

Ens-ID: ens_1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ALAALALEULEUAA1 - 1241 - 124
d_12ASNASNALAALAAA137 - 143137 - 143
d_13GLYGLYLYSLYSAA145 - 151145 - 151
d_21ALAALALEULEUBB1 - 1241 - 124
d_22ASNASNALAALABB137 - 143137 - 143
d_23GLYGLYLYSLYSBB145 - 151145 - 151
d_31ALAALALEULEUCC1 - 1241 - 124
d_32ASNASNALAALACC137 - 143137 - 143
d_33GLYGLYLYSLYSCC145 - 151145 - 151
d_41ALAALAALAALADD1 - 1431 - 143
d_42GLYGLYLYSLYSDD145 - 151145 - 151
d_51ALAALALEULEUEE1 - 1241 - 124
d_52ASNASNALAALAEE137 - 143137 - 143
d_53GLYGLYLYSLYSEE145 - 151145 - 151
d_61ALAALALEULEUFF1 - 1241 - 124
d_62ASNASNALAALAFF137 - 143137 - 143
d_63GLYGLYLYSLYSFF145 - 151145 - 151
d_71ALAALALEULEUGG1 - 1241 - 124
d_72ASNASNALAALAGG137 - 143137 - 143
d_73GLYGLYLYSLYSGG145 - 151145 - 151
d_81ALAALALEULEUHH1 - 1241 - 124
d_82ASNASNALAALAHH137 - 143137 - 143
d_83GLYGLYLYSLYSHH145 - 151145 - 151
d_91ALAALALEULEUII1 - 1241 - 124
d_92ASNASNALAALAII137 - 143137 - 143
d_93GLYGLYLYSLYSII145 - 151145 - 151
d_101ALAALALEULEUJJ1 - 1241 - 124
d_102ASNASNALAALAJJ137 - 143137 - 143
d_103GLYGLYLYSLYSJJ145 - 151145 - 151
d_111ALAALALEULEUKK1 - 1241 - 124
d_112ASNASNALAALAKK137 - 143137 - 143
d_113GLYGLYLYSLYSKK145 - 151145 - 151
d_121ALAALALEULEULL1 - 1241 - 124
d_122ASNASNALAALALL137 - 143137 - 143
d_123GLYGLYLYSLYSLL145 - 151145 - 151
d_131ALAALALEULEUMM1 - 1241 - 124
d_132ASNASNALAALAMM137 - 143137 - 143
d_133GLYGLYLYSLYSMM145 - 151145 - 151
d_141ALAALALEULEUNN1 - 1241 - 124
d_142ASNASNALAALANN137 - 143137 - 143
d_143GLYGLYLYSLYSNN145 - 151145 - 151
d_151ALAALALEULEUOO1 - 1241 - 124
d_152ASNASNALAALAOO137 - 143137 - 143
d_153GLYGLYLYSLYSOO145 - 151145 - 151
d_161ALAALALEULEUPP1 - 1241 - 124
d_162ASNASNALAALAPP137 - 143137 - 143
d_163GLYGLYLYSLYSPP145 - 151145 - 151

NCS oper:
IDCodeMatrixVector
1given(-0.050764861273, -0.776189827759, -0.628452289473), (-0.764627158319, -0.374598639179, 0.524424606866), (-0.642470417701, 0.507154030654, -0.574479374365)-10.5672991835, -20.4616818067, 9.53805590775
2given(0.997421306042, 0.0584922911039, 0.0415859367386), (-0.0597396444975, 0.997780594756, 0.0294118956284), (-0.0397732715315, -0.0318203804277, 0.998701932641)19.7683895121, 43.4292088482, 0.00527072394143
3given(-0.107557695365, -0.769997065083, -0.628916418875), (-0.77334790211, -0.332743010796, 0.539643503684), (-0.624791456784, 0.544414004715, -0.559686543523)8.40140149586, 23.0375647887, 10.6657129118
4given(-0.395027910599, 0.816550469175, 0.420949261953), (0.63942707988, 0.57339248564, -0.512205102403), (-0.659610460321, 0.0668310459476, -0.748630517634)105.68764634, -10.27380403, -14.8189472096
5given(-0.868535913757, 0.260734445203, 0.42150078956), (-0.179904202877, -0.958288276466, 0.222076691652), (0.461822308146, 0.11705181875, 0.87921500637)98.062435461, -32.0144183654, -16.007987388
6given(-0.387499761251, 0.830931736055, 0.39924476834), (0.638285374265, 0.554313393243, -0.534161439146), (-0.665158414236, 0.0478446662451, -0.745167881677)87.2885391694, -52.5951121813, -15.0345863782
7given(-0.868680554578, 0.244554717237, 0.430798194489), (-0.157661805882, -0.960912754684, 0.227572917658), (0.469613510308, 0.129767747005, 0.873283162997)79.2741673918, -74.0077792514, -15.6930779354
8given(0.00925830384583, -0.99978948813, -0.0183101948357), (-0.963545819654, -0.0138159434563, 0.267186401475), (-0.267383128182, 0.0151690188027, -0.963470894024)-1.80918771961, 35.3788606464, -62.8015948709
9given(0.812507817164, 0.294308994211, -0.503203003742), (-0.0661096578936, 0.904151133183, 0.422066631585), (0.579189571886, -0.309665859099, 0.75408653053)16.0108729432, 47.6034831698, -68.9576439928
10given(0.0239377329627, -0.99803357271, -0.0579307576779), (-0.966891956196, -0.0378393097775, 0.252365076187), (-0.254060878499, 0.0499717358123, -0.96589642076)-20.0921165642, -7.50043132056, -62.201129026
11given(0.825696268545, 0.278565948637, -0.490537138626), (-0.046086088076, 0.899973384173, 0.433501995689), (0.562229263376, -0.335334042472, 0.755942679945)-2.16901385954, 5.12083516079, -69.5751133036
12given(-0.612006915308, -0.183065690843, 0.769372788999), (-0.146866721774, -0.929609063335, -0.338019460093), (0.777095683716, -0.319865506428, 0.54204091741)54.082139812, -82.5322071186, -84.16842323
13given(-0.304928530362, 0.942143378534, -0.139228034737), (0.941232119642, 0.275825452249, -0.194942085878), (-0.14526075976, -0.190489302001, -0.970882658974)71.2901380639, -65.52876032, -79.984604142
14given(-0.602628879267, -0.164741294883, 0.780832081586), (-0.173076717308, -0.928189104904, -0.329407704015), (0.779026882591, -0.333654448942, 0.530840677513)72.4916414824, -40.1042105949, -84.7545345695
15given(-0.319238232399, 0.935936451132, -0.148694016076), (0.936778072324, 0.287933749644, -0.198849186646), (-0.143296176462, -0.202773556605, -0.968684205793)89.3262659039, -23.411388297, -80.3749068824

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Components

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Protein , 1 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein
Superoxide dismutase [Cu-Zn]


Mass: 15573.337 Da / Num. of mol.: 16 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00442, superoxide dismutase

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Non-polymers , 8 types, 1684 molecules

#2: Chemical
ChemComp-CU / COPPER (II) ION / Copper


Mass: 63.546 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Cu
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: 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
#6: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#7: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#8: Chemical ChemComp-H2S / HYDROSULFURIC ACID / HYDROGEN SULFIDE / Hydrogen sulfide


Mass: 34.081 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: H2S / Feature type: SUBJECT OF INVESTIGATION
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1643 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.22 Å3/Da / Density % sol: 44.55 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5.5 / Details: 25%PEG4000, 150mM ammonium sulfate and 100 mM MES

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97849 Å
DetectorType: DECTRIS PILATUS 300K / Detector: PIXEL / Date: Jun 21, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97849 Å / Relative weight: 1
ReflectionResolution: 1.88→50 Å / Num. obs: 163377 / % possible obs: 93.1 % / Redundancy: 3.7 % / Biso Wilson estimate: 18.99 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.059 / Rsym value: 0.059 / Net I/σ(I): 20.2
Reflection shellResolution: 1.88→1.91 Å / Rmerge(I) obs: 0.509 / Mean I/σ(I) obs: 2.5 / Num. unique obs: 8475 / CC1/2: 0.8883 / Rsym value: 0.509

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.88→30.68 Å / SU ML: 0.2281 / Cross valid method: FREE R-VALUE / σ(F): 1.98 / Phase error: 28.3745
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2445 7837 5.05 %
Rwork0.2009 147369 -
obs0.2031 155206 88.42 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 26.68 Å2
Refinement stepCycle: LAST / Resolution: 1.88→30.68 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17155 0 64 1643 18862
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.007217484
X-RAY DIFFRACTIONf_angle_d0.904623669
X-RAY DIFFRACTIONf_chiral_restr0.06212712
X-RAY DIFFRACTIONf_plane_restr0.0063165
X-RAY DIFFRACTIONf_dihedral_angle_d12.98026156
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AX-RAY DIFFRACTIONTorsion NCS0.459462028183
ens_1d_3AX-RAY DIFFRACTIONTorsion NCS0.30054697365
ens_1d_4AX-RAY DIFFRACTIONTorsion NCS0.465707077879
ens_1d_5AX-RAY DIFFRACTIONTorsion NCS0.39858838432
ens_1d_6AX-RAY DIFFRACTIONTorsion NCS0.500539859895
ens_1d_7AX-RAY DIFFRACTIONTorsion NCS0.421649261492
ens_1d_8AX-RAY DIFFRACTIONTorsion NCS0.468608162536
ens_1d_9AX-RAY DIFFRACTIONTorsion NCS0.485590557346
ens_1d_10AX-RAY DIFFRACTIONTorsion NCS0.406663416145
ens_1d_11AX-RAY DIFFRACTIONTorsion NCS0.476961249319
ens_1d_12AX-RAY DIFFRACTIONTorsion NCS0.383872880867
ens_1d_13AX-RAY DIFFRACTIONTorsion NCS0.470130162322
ens_1d_14AX-RAY DIFFRACTIONTorsion NCS0.306365855646
ens_1d_15AX-RAY DIFFRACTIONTorsion NCS0.451177475128
ens_1d_16AX-RAY DIFFRACTIONTorsion NCS0.275671941781
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.88-1.90.35261450.26782945X-RAY DIFFRACTION52.2
1.9-1.920.33621750.2523385X-RAY DIFFRACTION61.07
1.92-1.950.3242540.25433973X-RAY DIFFRACTION72.28
1.95-1.970.27242480.24564368X-RAY DIFFRACTION79.24
1.97-20.29812310.24714802X-RAY DIFFRACTION86.33
2-2.030.25942670.23795046X-RAY DIFFRACTION90.27
2.03-2.050.28752970.2425066X-RAY DIFFRACTION91.96
2.05-2.090.27373090.23815084X-RAY DIFFRACTION92.41
2.09-2.120.29462510.23665117X-RAY DIFFRACTION91.18
2.12-2.150.30362360.23824943X-RAY DIFFRACTION89.34
2.15-2.190.29652250.23744678X-RAY DIFFRACTION82.82
2.19-2.230.30352780.2255079X-RAY DIFFRACTION92.38
2.23-2.270.25662770.22475356X-RAY DIFFRACTION95.88
2.27-2.320.28073000.21665307X-RAY DIFFRACTION95.75
2.32-2.370.27582960.20615265X-RAY DIFFRACTION95.55
2.37-2.420.24532370.21255319X-RAY DIFFRACTION94.51
2.42-2.480.2682690.21555259X-RAY DIFFRACTION94.77
2.48-2.550.27432880.21745223X-RAY DIFFRACTION94.32
2.55-2.630.26472690.21865169X-RAY DIFFRACTION92.39
2.63-2.710.27693060.21854996X-RAY DIFFRACTION91.27
2.71-2.810.24882440.21484681X-RAY DIFFRACTION83.87
2.81-2.920.27872660.21715026X-RAY DIFFRACTION90.96
2.92-3.050.23753330.20715329X-RAY DIFFRACTION96.37
3.05-3.210.24292470.20155337X-RAY DIFFRACTION95.55
3.21-3.420.22092660.19665307X-RAY DIFFRACTION95.51
3.42-3.680.22222660.18265179X-RAY DIFFRACTION93.09
3.68-4.050.19142740.16374856X-RAY DIFFRACTION87.65
4.05-4.630.18092470.14495080X-RAY DIFFRACTION90.86
4.63-5.830.19813000.1535306X-RAY DIFFRACTION95.76
5.83-30.680.18592360.16544888X-RAY DIFFRACTION87.69

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