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- PDB-2w2w: PLCg2 Split Pleckstrin Homology (PH) Domain -

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Basic information

Entry
Database: PDB / ID: 2w2w
TitlePLCg2 Split Pleckstrin Homology (PH) Domain
Components1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
KeywordsHYDROLASE / PHOSPHOLIPASE C / PHOSPHOINOSITIDES / RHO GTPASES / RAC / SH2 DOMAIN / SH3 DOMAIN
Function / homology
Function and homology information


follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / positive regulation of dendritic cell cytokine production / antifungal innate immune response / phosphoinositide phospholipase C / positive regulation of interleukin-23 production / phosphorylation-dependent protein binding / phospholipid catabolic process / cellular response to lectin ...follicular B cell differentiation / inositol trisphosphate biosynthetic process / regulation of calcineurin-NFAT signaling cascade / positive regulation of dendritic cell cytokine production / antifungal innate immune response / phosphoinositide phospholipase C / positive regulation of interleukin-23 production / phosphorylation-dependent protein binding / phospholipid catabolic process / cellular response to lectin / positive regulation of I-kappaB phosphorylation / response to yeast / positive regulation of cell cycle G1/S phase transition / phosphatidylinositol metabolic process / Toll Like Receptor 4 (TLR4) Cascade / cell activation / positive regulation of neuroinflammatory response / positive regulation of phagocytosis, engulfment / phosphatidylinositol phospholipase C activity / Erythropoietin activates Phospholipase C gamma (PLCG) / phospholipase C activity / phosphatidylinositol biosynthetic process / macrophage activation involved in immune response / programmed cell death / cellular response to lipid / negative regulation of programmed cell death / regulation of canonical NF-kappaB signal transduction / positive regulation of macrophage cytokine production / positive regulation of reactive oxygen species biosynthetic process / positive regulation of NLRP3 inflammasome complex assembly / toll-like receptor signaling pathway / intracellular vesicle / positive regulation of epithelial cell migration / Dectin-2 family / Synthesis of IP3 and IP4 in the cytosol / Fc-epsilon receptor signaling pathway / stimulatory C-type lectin receptor signaling pathway / positive regulation of interleukin-10 production / phosphatidylinositol-mediated signaling / positive regulation of receptor internalization / regulation of lipid metabolic process / Generation of second messenger molecules / response to axon injury / positive regulation of type I interferon production / Role of phospholipids in phagocytosis / positive regulation of calcium-mediated signaling / release of sequestered calcium ion into cytosol / lipopolysaccharide-mediated signaling pathway / GPVI-mediated activation cascade / cellular response to calcium ion / positive regulation of interleukin-2 production / positive regulation of interleukin-12 production / phosphotyrosine residue binding / FCERI mediated Ca+2 mobilization / B cell differentiation / FCGR3A-mediated IL10 synthesis / protein tyrosine kinase binding / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / calcium-mediated signaling / FCERI mediated MAPK activation / B cell receptor signaling pathway / platelet activation / CLEC7A (Dectin-1) signaling / Wnt signaling pathway / positive regulation of DNA-binding transcription factor activity / ruffle membrane / Signaling by CSF1 (M-CSF) in myeloid cells / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / positive regulation of peptidyl-tyrosine phosphorylation / DAP12 signaling / positive regulation of NF-kappaB transcription factor activity / T cell receptor signaling pathway / scaffold protein binding / Potential therapeutics for SARS / positive regulation of MAPK cascade / intracellular signal transduction / membrane raft / positive regulation of gene expression / protein kinase binding / perinuclear region of cytoplasm / extracellular exosome / plasma membrane / cytoplasm / cytosol
Similarity search - Function
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2, SH3 domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma / PLC-gamma, C-terminal SH2 domain / PLC-gamma, N-terminal SH2 domain / Pleckstrin homology domain / Phosphoinositide phospholipase C family / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphatidylinositol-specific phospholipase C, Y domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. / Phospholipase C, catalytic domain (part); domain Y ...1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2, SH3 domain / Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma / PLC-gamma, C-terminal SH2 domain / PLC-gamma, N-terminal SH2 domain / Pleckstrin homology domain / Phosphoinositide phospholipase C family / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphatidylinositol-specific phospholipase C, Y domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. / Phospholipase C, catalytic domain (part); domain Y / Phosphatidylinositol-specific phospholipase C, X domain / Phosphatidylinositol-specific phospholipase C, X domain / Phospholipase C, catalytic domain (part); domain X / Phosphatidylinositol-specific phospholipase X-box domain profile. / PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / C2 domain superfamily / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / EF-hand domain pair / PH-like domain superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsOpaleye, O. / Bunney, T.D. / Roe, S.M. / Pearl, L.H.
CitationJournal: Mol.Cell / Year: 2009
Title: Structural Insights Into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2.
Authors: Bunney, T.D. / Opaleye, O. / Roe, S.M. / Vatter, P. / Baxendale, R.W. / Walliser, C. / Everett, K.L. / Josephs, M.B. / Christow, C. / Rodrigues-Lima, F. / Gierschik, P. / Pearl, L.H. / Katan, M.
History
DepositionNov 4, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 5, 2009Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.temp / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
B: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
C: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
D: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
E: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
F: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
G: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
H: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
I: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
J: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
K: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2
L: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)170,43412
Polymers170,43412
Non-polymers00
Water00
1
A: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
3
C: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
D: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
5
E: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
6
F: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
7
G: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
8
H: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
9
I: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
10
J: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
11
K: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
12
L: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2


Theoretical massNumber of molelcules
Total (without water)14,2031
Polymers14,2031
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)92.216, 106.017, 194.097
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
111
121

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
211CHAIN B AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
311CHAIN C AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
411CHAIN D AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
511CHAIN E AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
611CHAIN F AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
711CHAIN G AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
811CHAIN H AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
911CHAIN I AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
1011CHAIN J AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
1111CHAIN K AND (RESSEQ 7:42 OR RESSEQ 52: 83 OR RESSEQ 89:101 OR RESSEQ 106:112 )
1211CHAIN L AND (RESSEQ 7:12 OR RESSEQ 25: 38 OR RESSEQ 52:81 OR RESSEQ 91:101 OR RESSEQ 106:112 )

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Components

#1: Protein
1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2 / PHOSPHOINOSITIDE PHOSPHOLIPASE C / PHOSPHOLIPASE C-GAMMA-2 / PLC-GAMMA-2 / PLC-IV


Mass: 14202.820 Da / Num. of mol.: 12
Fragment: SPLIT PLECKSTRIN HOMOLOGY (SPPH), RESIDUES 471-515 AND 842-913
Mutation: YES
Source method: isolated from a genetically manipulated source
Details: TWO SH2 DOMAINS EXCISED FROM SEQUENCE AND CHAIN LINKED TOGETHER
Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm)
References: UniProt: P16885, phosphoinositide phospholipase C
Compound detailsENGINEERED RESIDUE IN CHAIN A, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN B, TYR 495 TO PHE ...ENGINEERED RESIDUE IN CHAIN A, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN B, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN C, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN D, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN E, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN F, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN G, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN H, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN I, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN J, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN K, TYR 495 TO PHE ENGINEERED RESIDUE IN CHAIN L, TYR 495 TO PHE
Sequence detailsINITIAL TAG LINKER AT START (GGGSGGS). TWO SH2 DOMAINS EXCISED FROM SEQUENCE AND CHAIN LINKED TOGETHER

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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: 3.1 Å3/Da / Density % sol: 60 % / Description: NONE
Crystal growTemperature: 293 K / pH: 7
Details: PLCSPPH(Y495F) WAS CRYSTALLIZED USING A PROTEIN CONCENTRATION OF 36 MG/ML WITH PRECIPITANT (20% PEG3350, 100 MM BIS-TRIS PROPANE PH 7.5) AT A CONSTANT TEMPERATURE OF 20C

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.92
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 13, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92 Å / Relative weight: 1
ReflectionResolution: 3.3→70 Å / Num. obs: 28821 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 85.51 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 7.1
Reflection shellResolution: 3.3→3.48 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 1.4 / % possible all: 95.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1UPQ

1upq


Resolution: 2.8→97.05 Å / SU ML: 0.61 / σ(F): 1.2 / Phase error: 42.75 / Stereochemistry target values: ML / Details: STRUCTURE IS INCREASING DISORDERED A TO L
RfactorNum. reflection% reflection
Rfree0.352 4099 5.1 %
Rwork0.303 --
obs0.306 80476 88.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 48.86 Å2 / ksol: 0.32 e/Å3
Displacement parametersBiso mean: 94.09 Å2
Baniso -1Baniso -2Baniso -3
1--9.5105 Å20 Å20 Å2
2--4.0687 Å2-0 Å2
3---5.4419 Å2
Refinement stepCycle: LAST / Resolution: 2.8→97.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9249 0 0 0 9249
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.019471
X-RAY DIFFRACTIONf_angle_d1.22612876
X-RAY DIFFRACTIONf_dihedral_angle_d19.6033227
X-RAY DIFFRACTIONf_chiral_restr0.0731415
X-RAY DIFFRACTIONf_plane_restr0.0081666
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A687X-RAY DIFFRACTIONPOSITIONAL
12B687X-RAY DIFFRACTIONPOSITIONAL0.085
13C685X-RAY DIFFRACTIONPOSITIONAL0.071
14D687X-RAY DIFFRACTIONPOSITIONAL0.091
15E685X-RAY DIFFRACTIONPOSITIONAL0.058
16F685X-RAY DIFFRACTIONPOSITIONAL0.076
17G681X-RAY DIFFRACTIONPOSITIONAL0.075
18H681X-RAY DIFFRACTIONPOSITIONAL0.071
19I681X-RAY DIFFRACTIONPOSITIONAL0.065
110J685X-RAY DIFFRACTIONPOSITIONAL0.069
111K681X-RAY DIFFRACTIONPOSITIONAL0.068
112L521X-RAY DIFFRACTIONPOSITIONAL0.063
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8002-2.83320.3544340.4148773X-RAY DIFFRACTION26
2.8332-2.86770.4249590.38791583X-RAY DIFFRACTION52
2.8677-2.9040.41131140.4071989X-RAY DIFFRACTION68
2.904-2.94220.3991070.39252319X-RAY DIFFRACTION78
2.9422-2.98260.43281470.40132531X-RAY DIFFRACTION85
2.9826-3.02520.39541360.39212572X-RAY DIFFRACTION87
3.0252-3.07030.40821500.37912665X-RAY DIFFRACTION90
3.0703-3.11830.43721180.38342680X-RAY DIFFRACTION89
3.1183-3.16940.36821360.37492646X-RAY DIFFRACTION91
3.1694-3.22410.41421430.37192695X-RAY DIFFRACTION91
3.2241-3.28270.39751650.37262719X-RAY DIFFRACTION92
3.2827-3.34590.41541870.36552673X-RAY DIFFRACTION92
3.3459-3.41420.32191350.36052764X-RAY DIFFRACTION92
3.4142-3.48840.42731210.37122725X-RAY DIFFRACTION93
3.4884-3.56950.38811900.37072762X-RAY DIFFRACTION94
3.5695-3.65880.44421550.37572777X-RAY DIFFRACTION94
3.6588-3.75770.37051400.3462820X-RAY DIFFRACTION96
3.7577-3.86830.43611450.32622856X-RAY DIFFRACTION95
3.8683-3.99320.34862010.30362795X-RAY DIFFRACTION96
3.9932-4.13590.28561480.29482864X-RAY DIFFRACTION97
4.1359-4.30150.34561430.27942876X-RAY DIFFRACTION97
4.3015-4.49730.28581470.24992899X-RAY DIFFRACTION98
4.4973-4.73440.29881430.25522923X-RAY DIFFRACTION98
4.7344-5.0310.34041360.24262949X-RAY DIFFRACTION98
5.031-5.41940.30821450.24532911X-RAY DIFFRACTION98
5.4194-5.96470.29171970.24092866X-RAY DIFFRACTION99
5.9647-6.82760.3141640.2482905X-RAY DIFFRACTION98
6.8276-8.60130.25931620.242898X-RAY DIFFRACTION98
8.6013-97.10680.29671310.26172942X-RAY DIFFRACTION98

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