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- PDB-5pzx: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosph... -

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Basic information

Entry
Database: PDB / ID: 5pzx
TitleHuman liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[4-methoxy-3-(2-methylpropyl)phenyl]sulfonylurea
ComponentsFructose-1,6-bisphosphatase 1Fructose 1,6-bisphosphatase
KeywordsHYDROLASE/HYDROLASE INHIBITOR / D3R docking / HYDROLASE-HYDROLASE INHIBITOR complex
Function / homology
Function and homology information


sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / negative regulation of Ras protein signal transduction / Gluconeogenesis / fructose 1,6-bisphosphate metabolic process / cellular response to magnesium ion / monosaccharide binding / fructose metabolic process / fructose 6-phosphate metabolic process ...sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / negative regulation of Ras protein signal transduction / Gluconeogenesis / fructose 1,6-bisphosphate metabolic process / cellular response to magnesium ion / monosaccharide binding / fructose metabolic process / fructose 6-phosphate metabolic process / negative regulation of glycolytic process / regulation of gluconeogenesis / AMP binding / dephosphorylation / gluconeogenesis / negative regulation of cell growth / cellular response to xenobiotic stimulus => GO:0071466 / RNA polymerase II-specific DNA-binding transcription factor binding / negative regulation of transcription by RNA polymerase II / extracellular exosome / identical protein binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Fructose-1,6-bisphosphatase / Fructose-1-6-bisphosphatase active site. / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase, C-terminal domain / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1,6-bisphosphatase class 1 / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 ...Fructose-1,6-bisphosphatase / Fructose-1-6-bisphosphatase active site. / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase, C-terminal domain / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1,6-bisphosphatase class 1 / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 / Fructose-1,6-Bisphosphatase; Chain A, domain 1 / D-Maltodextrin-Binding Protein; domain 2 / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-94S / Fructose-1,6-bisphosphatase 1 / Fructose-bisphosphatase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.75 Å
Model detailsFor D3R project
AuthorsRuf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G. / Yang, H. / Shao, C. / Burley, S.K.
CitationJournal: To be published
Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[4-methoxy-3-(2- ...Title: Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[4-methoxy-3-(2-methylpropyl)phenyl]sulfonylurea
Authors: Ruf, A. / Joseph, C. / Alker, A. / Banner, D. / Tetaz, T. / Benz, J. / Kuhn, B. / Rudolph, M.G.
History
DepositionApr 18, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 9, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 16, 2019Group: Data collection / Category: diffrn_radiation / Item: _diffrn_radiation.pdbx_diffrn_protocol
Revision 1.2Feb 6, 2019Group: Data collection / Database references / Structure summary
Category: audit_author / citation_author / Item: _audit_author.name / _citation_author.name
Revision 1.3Feb 10, 2021Group: Structure summary / Category: audit_author / Item: _audit_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fructose-1,6-bisphosphatase 1
B: Fructose-1,6-bisphosphatase 1
C: Fructose-1,6-bisphosphatase 1
D: Fructose-1,6-bisphosphatase 1
E: Fructose-1,6-bisphosphatase 1
F: Fructose-1,6-bisphosphatase 1
G: Fructose-1,6-bisphosphatase 1
H: Fructose-1,6-bisphosphatase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)298,46216
Polymers294,8758
Non-polymers3,5878
Water4,125229
1
A: Fructose-1,6-bisphosphatase 1
B: Fructose-1,6-bisphosphatase 1
C: Fructose-1,6-bisphosphatase 1
D: Fructose-1,6-bisphosphatase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)149,2318
Polymers147,4384
Non-polymers1,7934
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16010 Å2
ΔGint-79 kcal/mol
Surface area44050 Å2
MethodPISA
2
E: Fructose-1,6-bisphosphatase 1
F: Fructose-1,6-bisphosphatase 1
G: Fructose-1,6-bisphosphatase 1
H: Fructose-1,6-bisphosphatase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)149,2318
Polymers147,4384
Non-polymers1,7934
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15980 Å2
ΔGint-79 kcal/mol
Surface area44260 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)66.363, 284.602, 83.312
Angle α, β, γ (deg.)90.000, 97.710, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 9 through 61 or resid 72...
21(chain B and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))
31(chain C and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))
41(chain D and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))
51(chain E and (resid 9 through 61 or resid 72...
61(chain F and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))
71(chain G and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))
81(chain H and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 9 through 61 or resid 72...A9 - 61
121(chain A and (resid 9 through 61 or resid 72...A72 - 139
131(chain A and (resid 9 through 61 or resid 72...A141 - 176
141(chain A and (resid 9 through 61 or resid 72...A178 - 335
211(chain B and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))B9 - 139
221(chain B and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))B141 - 176
231(chain B and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))B178 - 335
311(chain C and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))C9 - 139
321(chain C and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))C141 - 176
331(chain C and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))C178 - 335
411(chain D and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))D9 - 139
421(chain D and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))D141 - 176
431(chain D and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))D178 - 335
511(chain E and (resid 9 through 61 or resid 72...E9 - 61
521(chain E and (resid 9 through 61 or resid 72...E72 - 139
531(chain E and (resid 9 through 61 or resid 72...E141 - 176
541(chain E and (resid 9 through 61 or resid 72...E178 - 335
611(chain F and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))F9 - 139
621(chain F and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))F141 - 176
631(chain F and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))F178 - 335
711(chain G and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))G9 - 139
721(chain G and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))G141 - 176
731(chain G and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))G178 - 335
811(chain H and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))H9 - 139
821(chain H and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))H141 - 176
831(chain H and (resid 9 through 139 or resid 141 through 176 or resid 178 through 335))H178 - 335

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Components

#1: Protein
Fructose-1,6-bisphosphatase 1 / Fructose 1,6-bisphosphatase / Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6- ...Growth-inhibiting protein 17 / cDNA FLJ75786 / highly similar to Homo sapiens fructose-1 / 6-bisphosphatase 1 (FBP1) / mRNA


Mass: 36859.418 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FBP1, hCG_1640493 / Production host: Escherichia coli (E. coli)
References: UniProt: Q2TU34, UniProt: P09467*PLUS, fructose-bisphosphatase
#2: Chemical
ChemComp-94S / N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-4-methoxy-3-(2-methylpropyl)benzene-1-sulfonamide


Mass: 448.355 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C15H18BrN3O4S2
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 229 / Source method: isolated from a natural source / Formula: H2O

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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: 2.73 Å3/Da / Density % sol: 54.96 %
Crystal growTemperature: 300 K / Method: vapor diffusion, sitting drop / pH: 7
Details: 0.1M HEPES pH 7.0, 0.1M AMMONIUM ACETATE, 12%-25% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.987 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Dec 6, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.987 Å / Relative weight: 1
ReflectionResolution: 2.75→29.898 Å / Num. obs: 78913 / % possible obs: 99.88 %

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.23data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.75→29.898 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.25 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2511 3964 5.02 %
Rwork0.1786 74949 -
obs0.1823 78913 99.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 166.56 Å2 / Biso mean: 57.4605 Å2 / Biso min: 11.86 Å2
Refinement stepCycle: final / Resolution: 2.75→29.898 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19440 0 200 229 19869
Biso mean--67.73 41.4 -
Num. residues----2540
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00820029
X-RAY DIFFRACTIONf_angle_d1.09727062
X-RAY DIFFRACTIONf_chiral_restr0.0643055
X-RAY DIFFRACTIONf_plane_restr0.0073450
X-RAY DIFFRACTIONf_dihedral_angle_d11.69712166
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A12124X-RAY DIFFRACTION10.355TORSIONAL
12B12124X-RAY DIFFRACTION10.355TORSIONAL
13C12124X-RAY DIFFRACTION10.355TORSIONAL
14D12124X-RAY DIFFRACTION10.355TORSIONAL
15E12124X-RAY DIFFRACTION10.355TORSIONAL
16F12124X-RAY DIFFRACTION10.355TORSIONAL
17G12124X-RAY DIFFRACTION10.355TORSIONAL
18H12124X-RAY DIFFRACTION10.355TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 28

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.75-2.78350.36191360.27332623275998
2.7835-2.81870.36121290.271626322761100
2.8187-2.85580.36771640.264926632827100
2.8558-2.89490.35611620.257927052867100
2.8949-2.93620.29531490.239626342783100
2.9362-2.980.31131430.225426982841100
2.98-3.02650.32621410.2326582799100
3.0265-3.07610.3141320.222826962828100
3.0761-3.12910.29141110.226926782789100
3.1291-3.18590.29931550.218626892844100
3.1859-3.24710.31571200.211926612781100
3.2471-3.31330.28241290.206227412870100
3.3133-3.38530.28981470.204126032750100
3.3853-3.46390.28571530.195927072860100
3.4639-3.55040.26531150.185427062821100
3.5504-3.64620.24061430.183826792822100
3.6462-3.75330.26481620.175826332795100
3.7533-3.87420.25781480.179526822830100
3.8742-4.01240.24291490.163826502799100
4.0124-4.17260.22271400.156927382878100
4.1726-4.3620.22351350.154626652800100
4.362-4.59120.21421660.138626352801100
4.5912-4.87770.21071240.128827042828100
4.8777-5.25240.19591410.139926922833100
5.2524-5.77760.20961260.157726812807100
5.7776-6.60570.24981540.172927182872100
6.6057-8.2930.23371400.158326992839100
8.293-29.90020.19211500.157326792829100
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)
10.0989-0.0397-0.04990.01720.01670.015-0.02180.08490.03910.017-0.0364-0.1047-0.1045-0.004600.3444-0.0157-0.01920.29640.06390.299836.856316.015-5.6354
20.0677-0.0848-0.01850.12930.00770.0346-0.07930.09920.0423-0.37580.03780.1691-0.07750.01490.03020.159-0.0065-0.13140.12320.08390.278719.246422.7951-8.0757
30.0541-0.0131-0.00020.01070.01130.0087-0.0275-0.03970.1574-0.07450.04140.114-0.177-0.0586-0.00040.395-0.0182-0.14080.14780.03390.372317.442931.3171-10.4198
40.127-0.1122-0.00210.0895-0.00680.0650.1077-0.1352-0.2055-0.0820.03970.1794-0.00060.00590.1264-0.26520.09720.08590.19490.06830.287111.5102-1.444815.1002
50.03820.0541-0.00970.05050.00010.1488-0.0775-0.08180.02250.1835-0.05250.0986-0.123-0.0167-0.03250.13880.01830.04350.23340.00580.303911.28669.487120.8668
60.007-0.0051-0.00660.00010.00180.02460.05950.02950.049-0.03110.05610.03720.00260.08890.00650.18650.1294-0.03580.2822-0.09010.62492.410832.14059.647
70.02360.0107-0.04110.0238-0.03790.03950.0537-0.1153-0.03680.09880.0570.0998-0.0635-0.0440.05290.08950.13390.01360.3478-0.02760.62680.264119.065417.5322
80.0110.0130.02230.13630.04970.044-0.0363-0.013-0.0476-0.23990.01390.0441-0.05770.0980.00010.3310.0480.03790.28150.0650.198638.9648-9.743-12.4291
90.1324-0.0870.05960.1269-0.18970.36770.08970.07050.0483-0.235-0.0723-0.03470.42190.03070.09540.00690.06040.11830.27710.07720.279556.4456-21.7219-4.1514
100.1109-0.11520.06850.1849-0.02550.0545-0.09990.02660.08270.15470.007-0.0798-0.0831-0.0881-0.0090.14930.04620.03940.2707-0.01290.2137.0534-7.481826.4789
110.03680.0433-0.04180.0251-0.03150.0371-0.0218-0.02740.01080.06850.04330.01020.10530.0926-00.1680.0691-0.00730.2230.04170.236541.9113-26.830114.5266
120.0123-0.028-0.0060.030.0120.0091-0.1239-0.04030.0417-0.1022-0.0056-0.02960.18440.023200.31980.07110.02120.31530.02580.310847.2614-26.969824.8648
130.0150.04540.00440.05950.0210.00990.1490.0096-0.09170.07570.0599-0.0962-0.15810.09270.00510.460.0055-0.01030.34990.03220.3001-1.235251.095142.3287
140.0884-0.0247-0.0570.05120.06420.0912-0.13620.043-0.32130.034-0.03940.05340.06520.1323-0.0290.5737-0.0067-0.06780.26880.10490.3867-5.325641.518345.9919
15-0.0003-0.0011-0.0010.02060.03090.06220.0012-0.0824-0.22420.11920.05360.1295-0.2219-0.02440.00020.3821-0.05110.00590.2506-0.00210.4695-24.78743.604238.0628
16-0.00250.01340.00010.0146-0.00160.0163-0.01320.0015-0.07760.0196-0.1033-0.05730.0555-0.081700.41-0.09170.02040.33830.04050.5385-21.549934.360945.4246
170.0275-0.0010.00350.0024-0.00250.01270.04730.05290.03110.0099-0.0027-0.0482-0.0393-0.0226-0.00010.4691-0.11050.03210.5872-0.01860.3464-5.703565.26553.7006
180.0620.0121-0.01120.03910.0130.01290.07350.0899-0.09270.14380.07850.1054-0.0829-0.1153-0.00010.45730.0564-0.01360.44410.02420.3461-22.314568.730819.2605
190.04890.0124-0.00510.013-0.01120.0168-0.00320.1625-0.2167-0.12520.0020.02-0.12570.0361-0.00010.45120.0256-0.0490.4982-0.07580.362-18.699957.107910.985
200.0083-0.00580.0002-0.00020.00610.0171-0.00570.0424-0.00890.10220.06060.0181-0.04230.0107-00.4333-0.0815-0.01470.4772-0.13010.6166-30.213440.236318.9964
210.01920.01260.01370.00380.0068-0.00250.04950.1436-0.1161-0.00810.13950.0941-0.00720.0825-00.40110.0316-0.09820.6091-0.14210.5634-31.453848.63788.8164
220.08850.0412-0.01790.04970.02090.00130.0304-0.10230.00650.04490.04180.10380.0064-0.1004-00.4131-0.06980.00290.25880.00450.2219-2.58275.402349.1096
230.1214-0.03690.09290.0446-0.04780.09490.0628-0.07210.04930.2128-0.02360.03060.03720.098600.318-0.05830.00320.2786-0.02260.219315.941984.781949.0516
240.07010.0396-0.00460.01850.0005-0.00040.07610.1239-0.1127-0.12010.063-0.02160.1406-0.1763-0.00010.463-0.0293-0.10060.38350.00090.26892.142970.747716.3805
250.0532-0.0192-0.02660.0546-0.02720.03650.0393-0.1407-0.0284-0.07870.0992-0.07390.12360.0227-00.5644-0.040.01470.3814-0.03190.236310.554777.221511.2841
260.0308-0.02440.00570.0552-0.06740.06040.110.00370.0375-0.05370.03980.00860.03980.0755-00.5061-0.08780.03880.39540.00160.367313.103795.831327.5201
270.01950.03070.01830.00980.01070.02720.00120.1205-0.0014-0.1629-0.00240.03580.0930.086100.5264-0.05690.01630.43030.0220.323517.74992.857517.0122
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 122 )A9 - 122
2X-RAY DIFFRACTION2chain 'A' and (resid 123 through 247 )A123 - 247
3X-RAY DIFFRACTION3chain 'A' and (resid 248 through 335 )A248 - 335
4X-RAY DIFFRACTION4chain 'B' and (resid 9 through 140 )B9 - 140
5X-RAY DIFFRACTION5chain 'B' and (resid 141 through 212 )B141 - 212
6X-RAY DIFFRACTION6chain 'B' and (resid 213 through 247 )B213 - 247
7X-RAY DIFFRACTION7chain 'B' and (resid 248 through 335 )B248 - 335
8X-RAY DIFFRACTION8chain 'C' and (resid 9 through 187 )C9 - 187
9X-RAY DIFFRACTION9chain 'C' and (resid 188 through 335 )C188 - 335
10X-RAY DIFFRACTION10chain 'D' and (resid 9 through 167 )D9 - 167
11X-RAY DIFFRACTION11chain 'D' and (resid 168 through 247 )D168 - 247
12X-RAY DIFFRACTION12chain 'D' and (resid 248 through 335 )D248 - 335
13X-RAY DIFFRACTION13chain 'E' and (resid 9 through 106 )E9 - 106
14X-RAY DIFFRACTION14chain 'E' and (resid 107 through 167 )E107 - 167
15X-RAY DIFFRACTION15chain 'E' and (resid 168 through 274 )E168 - 274
16X-RAY DIFFRACTION16chain 'E' and (resid 275 through 335 )E275 - 335
17X-RAY DIFFRACTION17chain 'F' and (resid 9 through 28 )F9 - 28
18X-RAY DIFFRACTION18chain 'F' and (resid 29 through 140 )F29 - 140
19X-RAY DIFFRACTION19chain 'F' and (resid 141 through 212 )F141 - 212
20X-RAY DIFFRACTION20chain 'F' and (resid 213 through 274 )F213 - 274
21X-RAY DIFFRACTION21chain 'F' and (resid 275 through 335 )F275 - 335
22X-RAY DIFFRACTION22chain 'G' and (resid 9 through 140 )G9 - 140
23X-RAY DIFFRACTION23chain 'G' and (resid 141 through 335 )G141 - 335
24X-RAY DIFFRACTION24chain 'H' and (resid 9 through 88 )H9 - 88
25X-RAY DIFFRACTION25chain 'H' and (resid 89 through 187 )H89 - 187
26X-RAY DIFFRACTION26chain 'H' and (resid 188 through 247 )H188 - 247
27X-RAY DIFFRACTION27chain 'H' and (resid 248 through 335 )H248 - 335

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