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- PDB-4d0m: Phosphatidylinositol 4-kinase III beta in a complex with Rab11a-G... -

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Basic information

Entry
Database: PDB / ID: 4d0m
TitlePhosphatidylinositol 4-kinase III beta in a complex with Rab11a-GTP- gamma-S and the Rab-binding domain of FIP3
Components
  • PHOSPHATIDYLINOSITOL 4-KINASE BETA
  • RAB11 FAMILY-INTERACTING PROTEIN 3
  • RAS-RELATED PROTEIN RAB-11A
KeywordsSIGNALING PROTEIN / PHOSPHOINOSITIDE / PHOSPHATIDYLINOSITOL 4-KINASE / LIPID KINASE / FAMILY OF RAB INTERACTING PROTEINS / FIP3 / RAB-BINDING DOMAIN / RBD / RAB11 / GTP / PIK93 / GOLGI / RECYCLING ENDOSOME
Function / homology
Function and homology information


regulation of early endosome to recycling endosome transport / regulation of protein localization to centrosome / protein localization to cleavage furrow / regulation of endocytic recycling / early endosome to recycling endosome transport / postsynaptic recycling endosome membrane / 1-phosphatidylinositol 4-kinase / 1-phosphatidylinositol 4-kinase activity / establishment of protein localization to organelle / establishment of vesicle localization ...regulation of early endosome to recycling endosome transport / regulation of protein localization to centrosome / protein localization to cleavage furrow / regulation of endocytic recycling / early endosome to recycling endosome transport / postsynaptic recycling endosome membrane / 1-phosphatidylinositol 4-kinase / 1-phosphatidylinositol 4-kinase activity / establishment of protein localization to organelle / establishment of vesicle localization / plasma membrane to endosome transport / negative regulation of adiponectin secretion / postsynaptic recycling endosome / positive regulation of mitotic cytokinetic process / regulation of cilium assembly / exosomal secretion / rough endoplasmic reticulum membrane / amyloid-beta clearance by transcytosis / astral microtubule organization / neurotransmitter receptor transport, endosome to postsynaptic membrane / melanosome transport / VxPx cargo-targeting to cilium / protein transmembrane transport / Synthesis of PIPs at the Golgi membrane / regulation of vesicle-mediated transport / myosin V binding / positive regulation of cilium assembly / RAB geranylgeranylation / Golgi to plasma membrane protein transport / phosphatidylinositol biosynthetic process / multivesicular body assembly / protein localization to cilium / endocytic recycling / establishment of protein localization to membrane / syntaxin binding / protein localization to cell surface / TBC/RABGAPs / dynein light intermediate chain binding / lysosome organization / mitotic metaphase chromosome alignment / phosphatidylinositol-mediated signaling / exocytosis / phosphatidylinositol phosphate biosynthetic process / inner ear development / cleavage furrow / positive regulation of epithelial cell migration / endocytic vesicle / mitotic spindle assembly / intercellular bridge / transport vesicle / vesicle-mediated transport / phagocytic vesicle / positive regulation of G2/M transition of mitotic cell cycle / 14-3-3 protein binding / multivesicular body / centriole / receptor-mediated endocytosis / Anchoring of the basal body to the plasma membrane / cytoplasmic vesicle membrane / small monomeric GTPase / regulation of cytokinesis / trans-Golgi network membrane / protein localization to plasma membrane / Translocation of SLC2A4 (GLUT4) to the plasma membrane / trans-Golgi network / recycling endosome / small GTPase binding / centriolar satellite / recycling endosome membrane / spindle pole / neuron projection development / Vasopressin regulates renal water homeostasis via Aquaporins / endocytic vesicle membrane / G protein activity / midbody / microtubule binding / cytoplasmic vesicle / protein-macromolecule adaptor activity / molecular adaptor activity / vesicle / mitochondrial outer membrane / endosome / ciliary basal body / cilium / Golgi membrane / cell division / GTPase activity / intracellular membrane-bounded organelle / centrosome / calcium ion binding / protein-containing complex binding / GTP binding / perinuclear region of cytoplasm / glutamatergic synapse / Golgi apparatus / signal transduction / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular exosome
Similarity search - Function
: / Rab-binding domain FIP-RBD / FIP-RBD, C-terminal domain superfamily / FIP domain / FIP-RBD domain profile. / : / PI4KB/PIK1, accessory (PIK) domain / : / small GTPase Rab1 family profile. / Phosphoinositide 3-kinase, accessory (PIK) domain ...: / Rab-binding domain FIP-RBD / FIP-RBD, C-terminal domain superfamily / FIP domain / FIP-RBD domain profile. / : / PI4KB/PIK1, accessory (PIK) domain / : / small GTPase Rab1 family profile. / Phosphoinositide 3-kinase, accessory (PIK) domain / Phosphatidylinositol kinase / PIK helical domain profile. / Phosphatidylinositol 3- and 4-kinases signature 1. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / EF-hand domain pair / Rab subfamily of small GTPases / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Small GTP-binding protein domain / Protein kinase-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Chem-093 / 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE / Rab11 family-interacting protein 3 / Ras-related protein Rab-11A / Phosphatidylinositol 4-kinase beta
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 6 Å
AuthorsBurke, J.E. / Inglis, A.J. / Perisic, O. / Masson, G.R. / McLaughlin, S.H. / Rutaganira, F. / Shokat, K.M. / Williams, R.L.
CitationJournal: Science / Year: 2014
Title: Structures of Pi4Kiiibeta Complexes Show Simultaneous Recruitment of Rab11 and its Effectors.
Authors: Burke, J.E. / Inglis, A.J. / Perisic, O. / Masson, G.R. / Mclaughlin, S.H. / Rutaganira, F. / Shokat, K.M. / Williams, R.L.
History
DepositionApr 29, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 28, 2014Provider: repository / Type: Initial release
Revision 1.1Jun 11, 2014Group: Database references
Revision 1.2Jun 18, 2014Group: Derived calculations
Revision 1.3Jun 20, 2018Group: Advisory / Data collection / Derived calculations
Category: pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues ...pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_conn / struct_conn_type
Item: _struct_conn_type.id
Revision 1.4Nov 21, 2018Group: Advisory / Data collection / Derived calculations
Category: pdbx_validate_close_contact / pdbx_validate_symm_contact ...pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_conn / struct_conn_type
Revision 1.5Dec 20, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / 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 / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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_label_asym_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PHOSPHATIDYLINOSITOL 4-KINASE BETA
B: RAS-RELATED PROTEIN RAB-11A
C: PHOSPHATIDYLINOSITOL 4-KINASE BETA
D: RAS-RELATED PROTEIN RAB-11A
E: RAB11 FAMILY-INTERACTING PROTEIN 3
F: RAB11 FAMILY-INTERACTING PROTEIN 3
G: PHOSPHATIDYLINOSITOL 4-KINASE BETA
H: RAS-RELATED PROTEIN RAB-11A
I: PHOSPHATIDYLINOSITOL 4-KINASE BETA
J: RAS-RELATED PROTEIN RAB-11A
K: RAB11 FAMILY-INTERACTING PROTEIN 3
L: RAB11 FAMILY-INTERACTING PROTEIN 3
M: PHOSPHATIDYLINOSITOL 4-KINASE BETA
N: RAS-RELATED PROTEIN RAB-11A
O: PHOSPHATIDYLINOSITOL 4-KINASE BETA
P: RAS-RELATED PROTEIN RAB-11A
Q: PHOSPHATIDYLINOSITOL 4-KINASE BETA
R: RAS-RELATED PROTEIN RAB-11A
S: PHOSPHATIDYLINOSITOL 4-KINASE BETA
T: RAS-RELATED PROTEIN RAB-11A
U: RAB11 FAMILY-INTERACTING PROTEIN 3
V: RAB11 FAMILY-INTERACTING PROTEIN 3
W: PHOSPHATIDYLINOSITOL 4-KINASE BETA
X: RAS-RELATED PROTEIN RAB-11A
Y: PHOSPHATIDYLINOSITOL 4-KINASE BETA
Z: RAS-RELATED PROTEIN RAB-11A
a: RAB11 FAMILY-INTERACTING PROTEIN 3
b: RAB11 FAMILY-INTERACTING PROTEIN 3
c: PHOSPHATIDYLINOSITOL 4-KINASE BETA
d: RAS-RELATED PROTEIN RAB-11A
e: RAB11 FAMILY-INTERACTING PROTEIN 3
f: RAB11 FAMILY-INTERACTING PROTEIN 3
g: PHOSPHATIDYLINOSITOL 4-KINASE BETA
h: RAS-RELATED PROTEIN RAB-11A
i: RAB11 FAMILY-INTERACTING PROTEIN 3
j: RAB11 FAMILY-INTERACTING PROTEIN 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,149,87372
Polymers1,138,43236
Non-polymers11,44136
Water00
1
A: PHOSPHATIDYLINOSITOL 4-KINASE BETA
B: RAS-RELATED PROTEIN RAB-11A
C: PHOSPHATIDYLINOSITOL 4-KINASE BETA
D: RAS-RELATED PROTEIN RAB-11A
E: RAB11 FAMILY-INTERACTING PROTEIN 3
F: RAB11 FAMILY-INTERACTING PROTEIN 3
O: PHOSPHATIDYLINOSITOL 4-KINASE BETA
P: RAS-RELATED PROTEIN RAB-11A
S: PHOSPHATIDYLINOSITOL 4-KINASE BETA
T: RAS-RELATED PROTEIN RAB-11A
U: RAB11 FAMILY-INTERACTING PROTEIN 3
V: RAB11 FAMILY-INTERACTING PROTEIN 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)383,29124
Polymers379,47712
Non-polymers3,81412
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2970 Å2
ΔGint-27.8 kcal/mol
Surface area29980 Å2
MethodPISA
2
G: PHOSPHATIDYLINOSITOL 4-KINASE BETA
H: RAS-RELATED PROTEIN RAB-11A
I: PHOSPHATIDYLINOSITOL 4-KINASE BETA
J: RAS-RELATED PROTEIN RAB-11A
K: RAB11 FAMILY-INTERACTING PROTEIN 3
L: RAB11 FAMILY-INTERACTING PROTEIN 3
M: PHOSPHATIDYLINOSITOL 4-KINASE BETA
N: RAS-RELATED PROTEIN RAB-11A
Q: PHOSPHATIDYLINOSITOL 4-KINASE BETA
R: RAS-RELATED PROTEIN RAB-11A
e: RAB11 FAMILY-INTERACTING PROTEIN 3
f: RAB11 FAMILY-INTERACTING PROTEIN 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)383,29124
Polymers379,47712
Non-polymers3,81412
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2970 Å2
ΔGint-27.8 kcal/mol
Surface area29980 Å2
MethodPISA
3
W: PHOSPHATIDYLINOSITOL 4-KINASE BETA
X: RAS-RELATED PROTEIN RAB-11A
Y: PHOSPHATIDYLINOSITOL 4-KINASE BETA
Z: RAS-RELATED PROTEIN RAB-11A
a: RAB11 FAMILY-INTERACTING PROTEIN 3
b: RAB11 FAMILY-INTERACTING PROTEIN 3
c: PHOSPHATIDYLINOSITOL 4-KINASE BETA
d: RAS-RELATED PROTEIN RAB-11A
g: PHOSPHATIDYLINOSITOL 4-KINASE BETA
h: RAS-RELATED PROTEIN RAB-11A
i: RAB11 FAMILY-INTERACTING PROTEIN 3
j: RAB11 FAMILY-INTERACTING PROTEIN 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)383,29124
Polymers379,47712
Non-polymers3,81412
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2970 Å2
ΔGint-27.8 kcal/mol
Surface area29980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)199.504, 134.465, 294.328
Angle α, β, γ (deg.)90.00, 90.33, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 2 types, 24 molecules ACGIMOQSWYcgBDHJNPRTXZdh

#1: Protein
PHOSPHATIDYLINOSITOL 4-KINASE BETA / PI4K-BETA / PI4KBETA / PTDINS 4-KINASE BETA / NPIK / PI4K92 / PHOSPHATIDYLINOSITOL 4-KINASE III BETA


Mass: 64593.141 Da / Num. of mol.: 12 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: HDX-OPTIMIZED DELETION VARIANT / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PACEBAC1-HSPI4KIIIB/PJB143 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm) / Strain (production host): SF9
References: UniProt: Q9UBF8, 1-phosphatidylinositol 4-kinase
#2: Protein
RAS-RELATED PROTEIN RAB-11A / RAB-11 / YL8 / RAB11A


Mass: 24691.818 Da / Num. of mol.: 12 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: POPTG/PJB88 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41 / References: UniProt: P62491, small monomeric GTPase

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Protein/peptide , 1 types, 12 molecules EFKLUVabefij

#3: Protein/peptide
RAB11 FAMILY-INTERACTING PROTEIN 3 / FIP3-RAB11 / RAB11-FIP3 / ARFOPHILIN-1 / EF HANDS-CONTAINING R AB-INTERACTING PROTEIN / EFERIN / MU- ...FIP3-RAB11 / RAB11-FIP3 / ARFOPHILIN-1 / EF HANDS-CONTAINING R AB-INTERACTING PROTEIN / EFERIN / MU-MB-17.148 / FIP3


Mass: 5584.360 Da / Num. of mol.: 12 / Fragment: RAB-BINDING DOMAIN / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PJB164-POPTG-HSFIP3 (713-756) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41 / References: UniProt: O75154

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Non-polymers , 3 types, 36 molecules

#4: Chemical
ChemComp-093 / N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE / PIK-93 / N-[(2Z)-5-(4-CHLORO-3-{[(2-HYDROXYETHYL)AMINO]SULFONYL}PHENYL)-4-METHYL-1,3-THIAZOL-2(3H)-YLIDENE]ACETAMIDE


Mass: 389.878 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C14H16ClN3O4S2
#5: Chemical
ChemComp-GSP / 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE


Mass: 539.246 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C10H16N5O13P3S
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: Mg

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Details

Sequence detailsTHREE HDX-OPTIMISED DELETIONS AND S294A MUTATION

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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: 2.9 Å3/Da / Density % sol: 58 % / Description: NONE
Crystal growDetails: 16% PEG 6K, 0.01 M NA CITRATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.968629
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 9, 2014 / Details: MIRRORS
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.968629 Å / Relative weight: 1
ReflectionResolution: 6→49.88 Å / Num. obs: 37822 / % possible obs: 95.9 % / Redundancy: 5.6 % / Rmerge(I) obs: 0.17 / Net I/σ(I): 17.8
Reflection shellResolution: 6→6.27 Å / Redundancy: 5.2 % / Rmerge(I) obs: 1.03 / Mean I/σ(I) obs: 2.2 / % possible all: 97

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Processing

Software
NameVersionClassification
REFMAC5.8.0069refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4D0L

4d0l


Resolution: 6→294.32 Å / Cor.coef. Fo:Fc: 0.862 / Cor.coef. Fo:Fc free: 0.789 / SU B: 262.603 / SU ML: 2.522 / Cross valid method: THROUGHOUT / ESU R Free: 3.049 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.U VALUES REFINED INDIVIDUALLY BECAUSE OF THE LOW RESOLUTION, WE MADE NO MANUAL READJUSTMENTS OF THE MODEL FOLLOWING RESTRAINED REFINEMENT WITH REFMAC.
RfactorNum. reflection% reflectionSelection details
Rfree0.35946 1925 5.2 %RANDOM
Rwork0.2533 ---
obs0.25888 35405 94.33 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 261.052 Å2
Baniso -1Baniso -2Baniso -3
1--11.35 Å2-0 Å24.49 Å2
2--0.69 Å20 Å2
3---10.61 Å2
Refinement stepCycle: LAST / Resolution: 6→294.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms65286 0 684 0 65970
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01966912
X-RAY DIFFRACTIONr_bond_other_d0.0060.0264890
X-RAY DIFFRACTIONr_angle_refined_deg1.3661.96890492
X-RAY DIFFRACTIONr_angle_other_deg1.0163148716
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.43358070
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.46823.7483090
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.2251512024
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.4615486
X-RAY DIFFRACTIONr_chiral_restr0.0710.210272
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0274430
X-RAY DIFFRACTIONr_gen_planes_other0.0050.0215648
X-RAY DIFFRACTIONr_nbd_refined0.2390.214161
X-RAY DIFFRACTIONr_nbd_other0.1880.261365
X-RAY DIFFRACTIONr_nbtor_refined0.1770.232098
X-RAY DIFFRACTIONr_nbtor_other0.0840.232488
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2990.2727
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.3420.235
X-RAY DIFFRACTIONr_metal_ion_refined0.330.236
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.7110.2385
X-RAY DIFFRACTIONr_symmetry_vdw_other0.5710.2561
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.8990.244
X-RAY DIFFRACTIONr_symmetry_hbond_other0.5940.212
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 6→6.156 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.448 130 -
Rwork0.313 2579 -
obs--93.25 %

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