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- PDB-8vyx: Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L... -

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Basic information

Entry
Database: PDB / ID: 8vyx
TitleCrystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with k-410
ComponentsEstrogen receptor
KeywordsNUCLEAR PROTEIN / Estrogen Receptor
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / epithelial cell development / prostate epithelial cord elongation / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / TFIIB-class transcription factor binding / androgen metabolic process / steroid hormone receptor signaling pathway / mammary gland alveolus development / estrogen receptor signaling pathway / cellular response to estrogen stimulus / estrogen response element binding / : / nuclear receptor-mediated steroid hormone signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / protein localization to chromatin / 14-3-3 protein binding / TBP-class protein binding / nitric-oxide synthase regulator activity / steroid binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / negative regulation of miRNA transcription / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / transcription coregulator binding / stem cell differentiation / nuclear estrogen receptor binding / SUMOylation of intracellular receptors / euchromatin / negative regulation of DNA-binding transcription factor activity / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Nuclear Receptor transcription pathway / response to estrogen / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / male gonad development / positive regulation of nitric oxide biosynthetic process / sequence-specific double-stranded DNA binding / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / ATPase binding / regulation of inflammatory response / fibroblast proliferation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / DNA-binding transcription activator activity, RNA polymerase II-specific / Estrogen-dependent gene expression / transcription regulator complex / Extra-nuclear estrogen signaling / calmodulin binding / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of gene expression / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of DNA-templated transcription / Golgi apparatus / enzyme binding / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) ...Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type
Similarity search - Domain/homology
: / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.69 Å
AuthorsMin, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. ...Min, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. / Izard, T. / Katzenellenbogen, B.S. / Katzenellenbogen, J.A. / Nettles, K.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2024
Title: Asymmetric allostery in estrogen receptor-alpha homodimers drives responses to the ensemble of estrogens in the hormonal milieu.
Authors: Min, C.K. / Nwachukwu, J.C. / Hou, Y. / Russo, R.J. / Papa, A. / Min, J. / Peng, R. / Kim, S.H. / Ziegler, Y. / Rangarajan, E.S. / Izard, T. / Katzenellenbogen, B.S. / Katzenellenbogen, J.A. / Nettles, K.W.
History
DepositionFeb 9, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Estrogen receptor
B: Estrogen receptor
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,1488
Polymers110,2464
Non-polymers1,9024
Water9,746541
1
A: Estrogen receptor
B: Estrogen receptor
hetero molecules


  • defined by author&software
  • 56.1 kDa, 2 polymers
Theoretical massNumber of molelcules
Total (without water)56,0744
Polymers55,1232
Non-polymers9512
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4850 Å2
ΔGint-19 kcal/mol
Surface area18740 Å2
MethodPISA
2
C: Estrogen receptor
D: Estrogen receptor
hetero molecules


  • defined by author&software
  • 56.1 kDa, 2 polymers
Theoretical massNumber of molelcules
Total (without water)56,0744
Polymers55,1232
Non-polymers9512
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4770 Å2
ΔGint-17 kcal/mol
Surface area19480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.809, 58.867, 94.127
Angle α, β, γ (deg.)86.75, 74.98, 62.91
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Estrogen receptor / ER / ER-alpha / Estradiol receptor / Nuclear receptor subfamily 3 group A member 1


Mass: 27561.377 Da / Num. of mol.: 4 / Mutation: L372S, L536S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P03372
#2: Chemical
ChemComp-A1AHU / 4,4'-[(1S,4S,5R)-5-(3,4-dihydroquinoline-1(2H)-sulfonyl)-7-oxabicyclo[2.2.1]hept-2-ene-2,3-diyl]diphenol


Mass: 475.556 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H25NO5S / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 541 / 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: 2.33 Å3/Da / Density % sol: 47.13 %
Crystal growTemperature: 298 K / Method: evaporation
Details: 20-25% PEG 3350, 200 mM MgCl2, 0.1 M Bis-Tris/Hepes/Tris-HCl

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Feb 12, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.69→33.101 Å / Num. obs: 75467 / % possible obs: 83.2 % / Redundancy: 7.1 % / CC1/2: 0.971 / Net I/σ(I): 6.2
Reflection shellResolution: 1.693→1.831 Å / Num. unique obs: 3774 / CC1/2: 0.143

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.69→33.1 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 28.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2462 3718 4.93 %
Rwork0.2086 --
obs0.2105 75444 68.28 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.69→33.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7169 0 136 541 7846
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.027451
X-RAY DIFFRACTIONf_angle_d2.0810109
X-RAY DIFFRACTIONf_dihedral_angle_d17.541070
X-RAY DIFFRACTIONf_chiral_restr0.0991195
X-RAY DIFFRACTIONf_plane_restr0.0151239
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.69-1.710.596380.3171127X-RAY DIFFRACTION3
1.71-1.740.4017180.3026250X-RAY DIFFRACTION7
1.74-1.760.3451230.2826393X-RAY DIFFRACTION10
1.76-1.790.3118310.2771692X-RAY DIFFRACTION17
1.79-1.810.3263540.27011092X-RAY DIFFRACTION28
1.81-1.840.3058720.27051699X-RAY DIFFRACTION43
1.84-1.870.28841060.24712025X-RAY DIFFRACTION53
1.87-1.90.29031190.25192237X-RAY DIFFRACTION57
1.9-1.940.27221180.23632420X-RAY DIFFRACTION63
1.94-1.970.26331430.22912681X-RAY DIFFRACTION68
1.97-2.010.28241430.22742839X-RAY DIFFRACTION74
2.01-2.060.25531530.23073081X-RAY DIFFRACTION79
2.06-2.110.29111430.21123059X-RAY DIFFRACTION78
2.11-2.160.24751910.20853461X-RAY DIFFRACTION90
2.16-2.220.23151810.19663552X-RAY DIFFRACTION91
2.22-2.280.27411940.19263567X-RAY DIFFRACTION92
2.28-2.360.22061920.18843560X-RAY DIFFRACTION91
2.36-2.440.25242000.19123419X-RAY DIFFRACTION89
2.44-2.540.24711630.1913294X-RAY DIFFRACTION85
2.54-2.650.24461590.19143514X-RAY DIFFRACTION91
2.65-2.790.2141920.20633635X-RAY DIFFRACTION93
2.79-2.970.22561690.20813569X-RAY DIFFRACTION92
2.97-3.20.26521840.21253478X-RAY DIFFRACTION90
3.2-3.520.23872050.20253409X-RAY DIFFRACTION88
3.52-4.030.22752100.18863591X-RAY DIFFRACTION94
4.03-5.070.22591790.19413450X-RAY DIFFRACTION88
5.07-33.10.26041680.25013632X-RAY DIFFRACTION93
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
15.9801-3.5747-0.72288.28140.19262.31440.0020.28090.1128-0.0607-0.1543-0.57350.09070.61230.18680.11-0.006-0.01880.27910.04920.159155.552728.131915.3234
25.3879-1.6797-0.5611.35930.78211.24440.110.05130.57370.1815-0.10030.1733-0.1319-0.22340.00580.1664-0.02920.03390.15710.00160.323832.497749.941312.8105
38.053-5.478-0.0464.2061-0.28210.78420.0152-0.19220.0128-0.16510.00980.1075-0.1044-0.01370.00440.1261-0.048-0.01160.0982-0.02820.138836.217842.09146.1069
42.8902-0.0802-0.52972.24260.41443.6258-0.02810.16010.0231-0.0814-0.09870.03820.05730.2370.08360.0661-0.01360.01070.0720.01740.106540.840430.74995.6476
54.02090.5867-0.90675.9814-1.89233.32890.1602-0.41590.04330.43390.17030.6224-0.5249-0.3706-0.22250.19350.03350.05830.2019-0.02320.240826.508343.019919.3133
66.4185-1.76282.0954.1042-1.06266.3127-0.2456-0.12740.11090.34930.0970.69930.1109-0.72710.04430.1779-0.01740.09920.1987-0.05260.240826.815232.624520.9523
72.6005-0.8136-0.69413.2380.34744.0414-0.0480.1198-0.09710.00820.00530.1390.32360.24780.01470.1023-0.01960.02140.06990.00960.139841.771325.51312.5464
81.64820.3368-0.53172.8356-0.07041.66150.04670.0578-0.0183-0.22860.0088-0.26260.09310.6238-0.0910.0830.02250.01120.17460.02840.148449.151619.249713.6623
94.4593-1.27873.84873.1953-2.96017.07710.0381-0.25890.1505-0.04050.05540.14660.0856-0.3885-0.10390.0516-0.0260.0340.0748-0.01940.123833.356623.676317.0627
108.11880.2470.46674.06541.3284.2980.20860.64620.4061-0.1391-0.1490.26470.0188-0.0169-0.10140.19970.0029-0.01660.19980.03460.160738.551536.4329-4.5285
113.36261.24882.74651.14431.09724.9813-0.1357-0.446-0.19050.04590.05720.14430.2542-0.26410.01350.1774-0.08-0.00310.0410.02320.158525.03340.588518.9837
122.84350.01021.54432.7159-0.70837.76260.04730.14970.1766-0.1160.0270.4021-0.1010.0666-0.19550.1193-0.0385-0.01740.12850.04970.166315.53995.37759.858
132.1118-0.1389-0.3121.3247-0.15413.1202-0.0037-0.10540.18540.14080.02370.0726-0.026-0.42080.00020.0909-0.02370.02860.1063-0.00380.150520.824712.290117.2331
144.84230.53040.52075.9988-0.11424.44690.02111.0852-0.3656-0.90370.3335-0.63670.64330.2283-0.15240.2226-0.08550.08460.1798-0.06460.241830.04622.1668-0.2529
155.6182-3.10480.83499.20442.08330.99410.00941.08530.3336-1.66170.1736-0.6863-0.2989-0.06170.09930.4901-0.1191-0.09220.3536-0.0610.138324.59955.1957-6.2572
165.0085-0.67561.16992.7039-0.84693.85650.10010.71230.1817-0.4515-0.0899-0.0970.29370.49070.1510.1880.00120.06310.20890.0120.072633.487410.93780.8501
172.8608-0.0645-0.06612.9514-0.22073.5078-0.0554-0.40970.15540.0849-0.04420.06210.01120.17380.09420.1415-0.072-0.00290.0133-0.0870.09829.601411.691518.2764
187.2-2.1483-1.42324.52321.39593.85530.1004-0.0110.20930.4331-0.2623-0.08260.0261-0.04140.16730.1522-0.02840.00990.10590.03350.102134.312511.666126.8624
197.8-2.65643.27962.8685-2.20774.38230.08370.13040.0147-0.2259-0.045-0.03110.1718-0.0357-0.03140.0973-0.03210.02970.0525-0.04210.116633.070816.391110.2214
202.67530.5233-0.06255.1364-2.80656.61880.04490.16780.0273-0.29490.36230.57480.0306-0.7464-0.20660.15870.02480.03460.3397-0.0150.34929.399314.935412.3142
211.6032-0.96330.24250.8386-0.0991.10450.06750.3363-0.3024-0.1215-0.0539-0.17430.12130.13370.00740.17230.08590.02670.2054-0.02250.13767.506412.173955.858
224.05813.2666-0.34942.6187-0.40090.87320.1593-0.0529-0.0347-0.0131-0.15480.05330.256-0.00820.06230.1440.07060.00490.0771-0.01730.16860.55789.879363.6951
233.03130.51560.36241.8836-0.03612.66960.0337-0.2448-0.12990.0506-0.0075-0.0109-0.03180.347-0.01550.08150.034-0.0170.10150.00560.088265.161121.278364.1554
240.81010.92480.05166.263-0.91472.1654-0.05010.2540.0224-0.53990.35670.84820.5023-0.3403-0.15310.368-0.0034-0.15970.1885-0.01690.288651.152413.404449.7564
252.48940.86011.27324.41240.45553.7156-0.1514-0.06910.077-0.0738-0.196-0.0674-0.11840.37820.20170.08720.02540.01640.09420.00860.126266.090126.818757.7305
261.3405-0.3017-1.16162.5375-0.0716.36360.01510.08330.2160.1743-0.224-0.1787-0.09350.60850.04610.06070.02020.0220.23350.00710.15773.649332.813157.8466
274.9981.601-4.09654.1821-3.06547.3545-0.05840.2547-0.0171-0.18910.06930.08530.2266-0.1814-0.08450.05430.0173-0.03530.0668-0.02170.075858.856729.022451.1078
289.56780.38991.13785.99771.47.52710.3826-0.2224-0.39080.6086-0.24560.3780.4347-0.0695-0.00470.2791-0.02360.03830.1630.0360.186563.016115.236674.2282
292.0468-0.19-1.68451.24470.91983.5069-0.259-0.0795-0.0515-0.09340.01850.1598-0.32480.0554-0.01750.21540.10840.00860.09820.03890.148848.098351.996353.2861
302.9788-0.0125-2.61451.71130.87096.09130.0654-0.2042-0.00330.0449-0.11260.14220.07880.28260.18480.16550.05-0.0010.15660.03610.142239.895846.731360.0906
311.8837-0.11250.14722.24720.25993.21930.004-0.1835-0.00730.19610.0616-0.0099-0.2257-0.4497-0.05490.06260.05880.01310.10460.03290.075147.742643.389660.5232
325.60131.0625-1.51053.9753-0.59826.63270.2451-0.8862-0.31130.3894-0.2341-0.0769-0.16230.3708-0.05920.1882-0.0027-0.0230.1817-0.02090.082657.726740.754768.971
333.41760.89651.06062.92940.09424.2149-0.03810.15130.0175-0.05660.0690.0938-0.055-0.10640.02460.08060.02380.02630.0760.01230.048453.022839.465950.9382
345.40982.13661.14273.2880.76673.5254-0.20120.1581-0.2748-0.36950.1194-0.2635-0.14570.04530.03030.1334-0.0040.02770.12960.06250.072457.166839.404142.1765
355.57330.3425-1.09862.3868-0.53943.7718-0.0458-0.02310.12710.18770.07320.1651-0.016-0.06190.08330.0770.0236-0.00860.0362-0.00410.063957.054835.545459.7925
363.2613-0.30831.06113.5655-1.61516.1455-0.0927-0.4734-0.02760.49120.33560.402-0.4415-0.99690.02740.2041-0.0142-0.00020.42340.00780.298233.721836.664658.2507
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 306 through 321 )
2X-RAY DIFFRACTION2chain 'A' and (resid 322 through 338 )
3X-RAY DIFFRACTION3chain 'A' and (resid 339 through 363 )
4X-RAY DIFFRACTION4chain 'A' and (resid 364 through 394 )
5X-RAY DIFFRACTION5chain 'A' and (resid 395 through 420 )
6X-RAY DIFFRACTION6chain 'A' and (resid 421 through 437 )
7X-RAY DIFFRACTION7chain 'A' and (resid 438 through 465 )
8X-RAY DIFFRACTION8chain 'A' and (resid 466 through 496 )
9X-RAY DIFFRACTION9chain 'A' and (resid 497 through 525 )
10X-RAY DIFFRACTION10chain 'A' and (resid 526 through 546 )
11X-RAY DIFFRACTION11chain 'B' and (resid 306 through 341 )
12X-RAY DIFFRACTION12chain 'B' and (resid 342 through 363 )
13X-RAY DIFFRACTION13chain 'B' and (resid 364 through 394 )
14X-RAY DIFFRACTION14chain 'B' and (resid 395 through 405 )
15X-RAY DIFFRACTION15chain 'B' and (resid 406 through 421 )
16X-RAY DIFFRACTION16chain 'B' and (resid 422 through 437 )
17X-RAY DIFFRACTION17chain 'B' and (resid 438 through 467 )
18X-RAY DIFFRACTION18chain 'B' and (resid 468 through 496 )
19X-RAY DIFFRACTION19chain 'B' and (resid 497 through 527 )
20X-RAY DIFFRACTION20chain 'B' and (resid 528 through 546 )
21X-RAY DIFFRACTION21chain 'C' and (resid 306 through 338 )
22X-RAY DIFFRACTION22chain 'C' and (resid 339 through 363 )
23X-RAY DIFFRACTION23chain 'C' and (resid 364 through 394 )
24X-RAY DIFFRACTION24chain 'C' and (resid 395 through 437 )
25X-RAY DIFFRACTION25chain 'C' and (resid 438 through 465 )
26X-RAY DIFFRACTION26chain 'C' and (resid 466 through 493 )
27X-RAY DIFFRACTION27chain 'C' and (resid 494 through 524 )
28X-RAY DIFFRACTION28chain 'C' and (resid 525 through 546 )
29X-RAY DIFFRACTION29chain 'D' and (resid 305 through 341 )
30X-RAY DIFFRACTION30chain 'D' and (resid 342 through 363 )
31X-RAY DIFFRACTION31chain 'D' and (resid 364 through 420 )
32X-RAY DIFFRACTION32chain 'D' and (resid 421 through 438 )
33X-RAY DIFFRACTION33chain 'D' and (resid 439 through 465 )
34X-RAY DIFFRACTION34chain 'D' and (resid 466 through 496 )
35X-RAY DIFFRACTION35chain 'D' and (resid 497 through 527 )
36X-RAY DIFFRACTION36chain 'D' and (resid 528 through 545 )

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