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- PDB-6aj4: Crystal structure of the DHR-2 domain of DOCK7 in complex with Cdc42 -

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Basic information

Entry
Database: PDB / ID: 6aj4
TitleCrystal structure of the DHR-2 domain of DOCK7 in complex with Cdc42
Components
  • Cell division control protein 42 homolog
  • Dedicator of cytokinesis protein 7
KeywordsSIGNALING PROTEIN / DOCK / GEF / DHR-2 / GTPase / Rho / Rac / Cdc42
Function / homology
Function and homology information


establishment of neuroblast polarity / interkinetic nuclear migration / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction ...establishment of neuroblast polarity / interkinetic nuclear migration / GBD domain binding / submandibular salivary gland formation / actin filament branching / Golgi transport complex / positive regulation of pinocytosis / modification of synaptic structure / endothelin receptor signaling pathway involved in heart process / Cdc42 protein signal transduction / cardiac neural crest cell migration involved in outflow tract morphogenesis / positive regulation of synapse structural plasticity / dendritic cell migration / storage vacuole / apolipoprotein A-I receptor binding / positive regulation of epithelial cell proliferation involved in lung morphogenesis / neuron fate determination / modulation by host of viral process / organelle transport along microtubule / regulation of attachment of spindle microtubules to kinetochore / positive regulation of pseudopodium assembly / Inactivation of CDC42 and RAC1 / cardiac conduction system development / GTP-dependent protein binding / regulation of filopodium assembly / basal part of cell / establishment of Golgi localization / leading edge membrane / neuropilin signaling pathway / positive regulation of intracellular protein transport / cell junction assembly / filopodium assembly / establishment of epithelial cell apical/basal polarity / regulation of modification of postsynaptic structure / dendritic spine morphogenesis / mitogen-activated protein kinase kinase kinase binding / embryonic heart tube development / thioesterase binding / regulation of stress fiber assembly / activation of GTPase activity / positive regulation of vascular associated smooth muscle cell migration / RHO GTPases activate KTN1 / regulation of lamellipodium assembly / nuclear migration / DCC mediated attractive signaling / MET activates RAP1 and RAC1 / negative regulation of cold-induced thermogenesis / adherens junction organization / sprouting angiogenesis / Wnt signaling pathway, planar cell polarity pathway / CD28 dependent Vav1 pathway / regulation of postsynapse organization / positive regulation of filopodium assembly / regulation of mitotic nuclear division / establishment or maintenance of cell polarity / phagocytosis, engulfment / RHOV GTPase cycle / small GTPase-mediated signal transduction / heart contraction / Myogenesis / RHOJ GTPase cycle / Golgi organization / RHOQ GTPase cycle / positive regulation of cytokinesis / RHO GTPases activate PAKs / CDC42 GTPase cycle / RHOU GTPase cycle / macrophage differentiation / RHOG GTPase cycle / regulation of neurogenesis / RHO GTPases Activate WASPs and WAVEs / RAC3 GTPase cycle / RAC2 GTPase cycle / RHO GTPases activate IQGAPs / spindle midzone / negative regulation of protein-containing complex assembly / phagocytic vesicle / positive regulation of lamellipodium assembly / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of stress fiber assembly / GPVI-mediated activation cascade / RAC1 GTPase cycle / EPHB-mediated forward signaling / substantia nigra development / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / axonogenesis / guanyl-nucleotide exchange factor activity / small monomeric GTPase / G protein activity / filopodium / positive regulation of DNA replication / secretory granule / actin filament organization / integrin-mediated signaling pathway / RHO GTPases Activate Formins / regulation of actin cytoskeleton organization / FCGR3A-mediated phagocytosis / EGFR downregulation / positive regulation of JNK cascade / MAPK6/MAPK4 signaling
Similarity search - Function
Dedicator of cytokinesis C, C2 domain / DOCK DHR2 domain, lobe C / Dedicator of cytokinesis C/D, N-terminal / Dedicator of cytokinesis C/D, N terminal / DOCKER, Lobe A / DOCKER, Lobe B / DOCKER, Lobe C / DHR-2, Lobe C / DHR-2, Lobe B / Dedicator of cytokinesis ...Dedicator of cytokinesis C, C2 domain / DOCK DHR2 domain, lobe C / Dedicator of cytokinesis C/D, N-terminal / Dedicator of cytokinesis C/D, N terminal / DOCKER, Lobe A / DOCKER, Lobe B / DOCKER, Lobe C / DHR-2, Lobe C / DHR-2, Lobe B / Dedicator of cytokinesis / C2 DOCK-type domain / DOCKER domain / Dedicator of cytokinesis, C-terminal, lobe A / Dedicator of cytokinesis, C-terminal, lobe C / DHR-2, Lobe A / C2 domain in Dock180 and Zizimin proteins / C2 DOCK-type domain profile. / DOCKER domain profile. / Cdc42 / Small GTPase Rho / small GTPase Rho family profile. / C2 domain superfamily / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Cell division control protein 42 homolog / Dedicator of cytokinesis protein 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.256 Å
AuthorsKukimoto-Niino, M. / Shirouzu, M.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science15K06987 Japan
CitationJournal: Structure / Year: 2019
Title: Structural Basis for the Dual Substrate Specificity of DOCK7 Guanine Nucleotide Exchange Factor.
Authors: Kukimoto-Niino, M. / Tsuda, K. / Ihara, K. / Mishima-Tsumagari, C. / Honda, K. / Ohsawa, N. / Shirouzu, M.
History
DepositionAug 27, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 20, 2019Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed
Revision 1.2May 22, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first
Revision 1.3Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Dedicator of cytokinesis protein 7
B: Cell division control protein 42 homolog
C: Dedicator of cytokinesis protein 7
D: Cell division control protein 42 homolog
E: Dedicator of cytokinesis protein 7
F: Cell division control protein 42 homolog
G: Dedicator of cytokinesis protein 7
H: Cell division control protein 42 homolog


Theoretical massNumber of molelcules
Total (without water)221,3568
Polymers221,3568
Non-polymers00
Water0
1
A: Dedicator of cytokinesis protein 7
B: Cell division control protein 42 homolog


Theoretical massNumber of molelcules
Total (without water)55,3392
Polymers55,3392
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4000 Å2
ΔGint-25 kcal/mol
Surface area22530 Å2
MethodPISA
2
C: Dedicator of cytokinesis protein 7
D: Cell division control protein 42 homolog


Theoretical massNumber of molelcules
Total (without water)55,3392
Polymers55,3392
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4110 Å2
ΔGint-25 kcal/mol
Surface area22510 Å2
MethodPISA
3
E: Dedicator of cytokinesis protein 7
F: Cell division control protein 42 homolog


Theoretical massNumber of molelcules
Total (without water)55,3392
Polymers55,3392
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4090 Å2
ΔGint-22 kcal/mol
Surface area22810 Å2
MethodPISA
4
G: Dedicator of cytokinesis protein 7
H: Cell division control protein 42 homolog


Theoretical massNumber of molelcules
Total (without water)55,3392
Polymers55,3392
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4080 Å2
ΔGint-24 kcal/mol
Surface area22600 Å2
MethodPISA
Unit cell
Length a, b, c (Å)196.460, 105.560, 118.140
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
Dedicator of cytokinesis protein 7


Mass: 33877.574 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: SF file contains Friedel pairs. / Source: (gene. exp.) Homo sapiens (human) / Gene: DOCK7, KIAA1771 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: Q96N67
#2: Protein
Cell division control protein 42 homolog / G25K GTP-binding protein


Mass: 21461.537 Da / Num. of mol.: 4 / Mutation: C188S
Source method: isolated from a genetically manipulated source
Details: SF file contains Friedel pairs. / Source: (gene. exp.) Homo sapiens (human) / Gene: CDC42 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P60953

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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: 2.77 Å3/Da / Density % sol: 55.55 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: PEG3350 and tri-potassium citrate monohydrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Jul 16, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.256→50 Å / Num. obs: 73997 / % possible obs: 99.4 % / Redundancy: 3.9 % / CC1/2: 0.996 / Rrim(I) all: 0.12 / Net I/σ(I): 11.9
Reflection shellResolution: 3.26→3.45 Å / Mean I/σ(I) obs: 1.7 / Num. unique obs: 11796 / CC1/2: 0.639 / Rrim(I) all: 0.96 / % possible all: 97.8

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Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3VHL
Resolution: 3.256→46.802 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 0.95 / Phase error: 27.6 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2588 3777 5.11 %
Rwork0.1837 --
obs0.1876 73981 99.47 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.256→46.802 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14684 0 0 0 14684
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01115020
X-RAY DIFFRACTIONf_angle_d1.28920320
X-RAY DIFFRACTIONf_dihedral_angle_d5.1559152
X-RAY DIFFRACTIONf_chiral_restr0.0612248
X-RAY DIFFRACTIONf_plane_restr0.0082624
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.256-3.29720.3531270.32122446X-RAY DIFFRACTION91
3.2972-3.34060.37761380.30252556X-RAY DIFFRACTION100
3.3406-3.38630.32241450.29062653X-RAY DIFFRACTION100
3.3863-3.43470.36511400.28092596X-RAY DIFFRACTION100
3.4347-3.48590.43611410.2762589X-RAY DIFFRACTION99
3.4859-3.54040.32941370.26032582X-RAY DIFFRACTION99
3.5404-3.59840.31181400.23452629X-RAY DIFFRACTION99
3.5984-3.66040.31081340.22422576X-RAY DIFFRACTION99
3.6604-3.7270.30871420.22152575X-RAY DIFFRACTION100
3.727-3.79860.31071410.19952630X-RAY DIFFRACTION100
3.7986-3.87610.27531430.20292615X-RAY DIFFRACTION100
3.8761-3.96040.27531410.20272581X-RAY DIFFRACTION100
3.9604-4.05240.28551440.19222632X-RAY DIFFRACTION100
4.0524-4.15370.28911410.18882596X-RAY DIFFRACTION100
4.1537-4.2660.31071390.17312607X-RAY DIFFRACTION100
4.266-4.39140.23641410.15772667X-RAY DIFFRACTION100
4.3914-4.5330.20451380.15352564X-RAY DIFFRACTION100
4.533-4.69490.19081440.14842586X-RAY DIFFRACTION100
4.6949-4.88270.24251410.14992627X-RAY DIFFRACTION100
4.8827-5.10460.23121380.15072614X-RAY DIFFRACTION100
5.1046-5.37340.23891390.14992625X-RAY DIFFRACTION100
5.3734-5.70950.26211370.16032599X-RAY DIFFRACTION100
5.7095-6.14950.21791430.16542623X-RAY DIFFRACTION100
6.1495-6.76670.28261430.18732603X-RAY DIFFRACTION100
6.7667-7.7420.24681400.18022606X-RAY DIFFRACTION100
7.742-9.73960.18341400.12882617X-RAY DIFFRACTION100
9.7396-46.80690.21941400.17942610X-RAY DIFFRACTION100
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)
14.05021.871-3.24376.08532.36446.4901-0.14010.9221-0.4635-0.9380.2168-0.0840.10720.9605-0.02470.58120.02470.00330.9096-0.06760.45687.83467.5708-0.506
27.1338-0.8232-4.56576.45925.71167.7471-0.1161.2326-0.1912-2.26790.85080.0343-1.46212.0557-0.57251.2056-0.48210.1231.4763-0.27210.68618.275414.8679-7.318
34.91910.97161.2334.63612.3063.5741-0.32920.75230.1622-0.82950.2720.1004-1.2063-0.2680.03880.80740.10.05030.67940.08050.4043-0.08719.57755.7498
43.432-0.7420.36245.6559-0.34884.8686-0.0826-0.67120.51940.13490.3365-0.0224-0.69190.0819-0.20450.5759-0.07010.05560.5992-0.15360.49317.089828.442530.4674
56.00161.0604-0.48617.5691-1.26279.5628-0.01040.4709-0.3418-0.0142-0.1135-0.2502-0.7211.16450.15790.55760.01930.02140.8211-0.15580.475719.198112.922122.8827
63.3104-1.39810.78757.51192.04544.16190.31720.4409-0.2923-0.1879-0.2182-0.108-0.32940.4403-0.11390.5733-0.12690.01360.8324-0.12490.61212.428114.643517.0521
73.28870.03510.69336.04610.78974.86850.1607-0.51980.30270.4274-0.0236-0.8998-0.07670.7889-0.11760.4418-0.0258-0.05810.9643-0.20530.667227.241912.283629.2014
83.38513.404-0.43537.0701-1.37830.3055-0.69692.50660.4858-3.68230.2087-1.3168-0.81822.58170.46431.5317-0.20790.59241.57140.19791.051637.342214.95366.7446
96.28933.0651-2.04156.32232.47526.4821-1.09960.4672-0.7969-1.62170.6351-0.68641.08310.97150.55080.5465-0.09120.21291.2469-0.06041.064939.38844.777317.5538
103.5156-1.1775-4.05719.8933-1.03665.35960.5724-0.2820.7177-1.246-0.4433-0.97320.70410.7014-0.01630.5950.01710.16940.5922-0.12640.572426.69365.252916.339
115.16131.9229-5.16075.3442-1.77385.2025-1.14880.7391-0.98-0.3229-0.4368-0.61421.0204-0.80961.17910.6230.0138-0.0060.6936-0.09820.578618.50581.251921.7495
124.30440.39571.76073.62831.55324.0119-0.2038-0.64980.51070.91450.331-0.5454-0.11320.76850.00350.65820.0397-0.00410.9789-0.24180.680413.689-6.024291.0116
135.2136-0.6616-0.05023.9358-0.08792.5119-0.103-0.41970.06630.38540.22590.03920.682-0.0292-0.11310.654-0.0628-0.03740.48220.00220.39825.9904-18.610982.5451
146.8595-4.63535.14425.0461-6.56468.7143-0.4316-0.47130.2490.17450.8820.2467-0.1983-1.1804-0.30610.5015-0.0369-0.00270.5089-0.010.482311.3129-23.407565.366
152.7589-0.18540.14537.2951-2.09044.7003-0.08070.4965-0.2877-0.86570.1769-0.5380.80250.3946-0.07220.696-0.0110.10150.6751-0.12680.5116.2962-25.024556.3559
160.7349-1.02392.35037.60420.8169.69380.0603-0.0349-0.18310.4203-0.0049-0.15710.630.679-0.13180.4387-0.1430.09990.4806-0.10580.699822.0783-6.503665.8099
170.5747-0.6539-1.74766.19760.21827.3290.1842-0.42610.51070.26420.0299-0.38650.15760.8602-0.34060.3463-0.00480.04360.6043-0.06670.693420.4569-9.669465.7152
181.2069-0.3861-1.57973.7311-1.13612.7531-0.09590.47890.0703-0.33390.2883-1.0676-0.36220.9877-0.22290.5676-0.11810.15180.859-0.13320.924532.3896-2.142959.3
198.4661-0.2266-4.87225.63670.81073.1664-0.6312-1.6341-0.271.22220.3645-1.8712-0.16320.54080.02550.65260.0367-0.16750.663-0.14210.985737.0884-0.120474.0241
208.4448-2.07429.89312.6723-0.74482.0015-2.2450.68872.595-0.31210.1408-1.5187-2.74820.39491.46720.994-0.27130.14030.7715-0.2521.633535.931910.684567.3508
214.10950.3091-0.73733.8994.87966.39760.6384-0.0451-0.34540.3677-0.4353-0.08570.36250.0877-0.25460.5472-0.0109-0.12070.3740.04350.769822.50243.663569.8451
227.2246-1.85212.26927.8139-3.90616.5430.7854-0.8351-1.01140.9626-0.11-0.79451.50680.7485-0.43551.50270.2297-0.42770.7634-0.09640.78427.317-34.06535.1834
236.7833-1.40671.9733.6133-2.60197.0480.1018-0.7304-1.04010.98410.38580.28210.5486-0.3731-0.45040.9160.0405-0.12030.6070.02390.648316.9625-31.230826.888
245.2081-1.01171.01025.1994.54196.31230.6635-0.0811-1.02490.67440.32350.04061.88840.4484-0.32051.31720.1882-0.25120.4618-0.02910.714317.0329-36.389722.1552
255.50483.12710.91256.58691.33721.35040.05841.6551-0.0496-0.60780.1572-0.08680.41410.6136-0.18640.78210.3844-0.05671.4169-0.02470.558222.8059-22.0079-0.7305
264.35450.65880.37923.15081.11411.76370.0530.8387-0.30830.22540.102-0.52740.05820.074-0.10990.76570.3601-0.09131.2442-0.17020.662541.7779-23.022111.298
278.591-5.7997-0.04434.01380.72534.33561.64980.0899-3.3777-0.3121-0.11020.85052.7522-0.1858-1.06251.50340.2638-0.74661.1663-0.46172.024850.831-43.658519.6308
283.0259-1.7508-0.13984.857-1.55190.81650.40130.1991-0.29410.3062-0.0476-0.83520.3506-0.1308-0.320.87550.3518-0.34581.1529-0.20130.865149.5683-25.528421.2529
295.31641.2282-0.67747.6628-2.83937.1574-0.11220.92870.2085-0.8832-0.265-0.8528-0.48630.09740.33160.8253-0.01920.10510.4433-0.01320.485315.078439.065953.4551
306.89136.1915-6.15745.7814-5.34515.73541.2771.47510.1953-0.5289-0.0540.4984-2.6042-1.0628-1.38051.45290.03740.0950.82370.13150.926415.168253.237756.5184
313.39630.7766-0.84293.75310.55276.47020.1690.05270.139-0.21190.1073-0.0463-0.5244-0.7441-0.17090.64060.1160.01360.4251-0.01540.47164.704734.547264.6148
327.1309-2.2759-1.26573.4264-1.41085.91210.0362-1.245-0.330.7983-0.1563-0.4052-0.56720.15820.12650.7987-0.2788-0.17560.6240.10580.61413.973128.043389.3303
333.588-1.49410.22311.5281-0.10062.36640.2007-0.35820.41240.3284-0.4444-1.0903-0.47770.54050.15540.7195-0.2819-0.22580.69410.21650.980532.108235.150378.0632
343.5301-1.93761.13387.96123.78783.669-0.00141.36521.3488-3.6879-1.77360.6528-2.80321.04441.85791.28130.0776-0.04181.19110.29441.501232.619254.011267.2465
352.40052.97851.76973.83792.91624.9658-0.74220.36411.4321-0.77880.07491.4542-3.08820.49440.21411.9193-0.4915-0.25931.09140.69721.860539.332859.385772.8604
364.86353.11140.46192.5910.85680.61620.00831.08820.4056-0.0801-0.7165-1.4275-0.46161.03580.33670.7103-0.217-0.08831.09050.50441.037538.761437.406167.5884
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1805 through 1853 )
2X-RAY DIFFRACTION2chain 'A' and (resid 1854 through 1877 )
3X-RAY DIFFRACTION3chain 'A' and (resid 1878 through 1960 )
4X-RAY DIFFRACTION4chain 'A' and (resid 1961 through 2079 )
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 24 )
6X-RAY DIFFRACTION6chain 'B' and (resid 25 through 49 )
7X-RAY DIFFRACTION7chain 'B' and (resid 50 through 115 )
8X-RAY DIFFRACTION8chain 'B' and (resid 116 through 132 )
9X-RAY DIFFRACTION9chain 'B' and (resid 133 through 148 )
10X-RAY DIFFRACTION10chain 'B' and (resid 149 through 164 )
11X-RAY DIFFRACTION11chain 'B' and (resid 165 through 178 )
12X-RAY DIFFRACTION12chain 'C' and (resid 1805 through 1877 )
13X-RAY DIFFRACTION13chain 'C' and (resid 1878 through 1960 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1961 through 1980 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1981 through 2079 )
16X-RAY DIFFRACTION16chain 'D' and (resid 1 through 25 )
17X-RAY DIFFRACTION17chain 'D' and (resid 26 through 67 )
18X-RAY DIFFRACTION18chain 'D' and (resid 68 through 104 )
19X-RAY DIFFRACTION19chain 'D' and (resid 105 through 138 )
20X-RAY DIFFRACTION20chain 'D' and (resid 139 through 149 )
21X-RAY DIFFRACTION21chain 'D' and (resid 150 through 178 )
22X-RAY DIFFRACTION22chain 'E' and (resid 1805 through 1862 )
23X-RAY DIFFRACTION23chain 'E' and (resid 1863 through 1908 )
24X-RAY DIFFRACTION24chain 'E' and (resid 1909 through 1960 )
25X-RAY DIFFRACTION25chain 'E' and (resid 1961 through 2079 )
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 115 )
27X-RAY DIFFRACTION27chain 'F' and (resid 116 through 132 )
28X-RAY DIFFRACTION28chain 'F' and (resid 133 through 178 )
29X-RAY DIFFRACTION29chain 'G' and (resid 1805 through 1854 )
30X-RAY DIFFRACTION30chain 'G' and (resid 1855 through 1877 )
31X-RAY DIFFRACTION31chain 'G' and (resid 1878 through 1960 )
32X-RAY DIFFRACTION32chain 'G' and (resid 1961 through 2079 )
33X-RAY DIFFRACTION33chain 'H' and (resid 1 through 115 )
34X-RAY DIFFRACTION34chain 'H' and (resid 116 through 125 )
35X-RAY DIFFRACTION35chain 'H' and (resid 126 through 138 )
36X-RAY DIFFRACTION36chain 'H' and (resid 139 through 178 )

+
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