[English] 日本語
Yorodumi
- EMDB-65778: Cryo-EM structure of the kinesin-2 tail domain in complex with KA... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-65778
TitleCryo-EM structure of the kinesin-2 tail domain in complex with KAP3 and APC
Map datasharpened map
Sample
  • Complex: Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC
    • Protein or peptide: Kinesin-like protein KIF3A
    • Protein or peptide: Kinesin-like protein KIF3B, N-terminally processed
    • Protein or peptide: Kinesin-associated protein 3
    • Protein or peptide: Adenomatous polyposis coli protein
KeywordsKinesin-2 motor Intracellular transport Kinesin-adaptor-cargo complex / MOTOR PROTEIN
Function / homology
Function and homology information


negative regulation of odontogenesis / axis specification / positive regulation of calcium-dependent cell-cell adhesion / opsin transport / epidermal stem cell homeostasis / positive regulation of axo-dendritic protein transport / positive regulation of establishment or maintenance of cell polarity regulating cell shape / kinesin II complex / : / intraciliary transport particle B binding ...negative regulation of odontogenesis / axis specification / positive regulation of calcium-dependent cell-cell adhesion / opsin transport / epidermal stem cell homeostasis / positive regulation of axo-dendritic protein transport / positive regulation of establishment or maintenance of cell polarity regulating cell shape / kinesin II complex / : / intraciliary transport particle B binding / Apoptotic cleavage of cellular proteins / periciliary membrane compartment / anterograde dendritic transport / Beta-catenin phosphorylation cascade / Activation of SMO / Disassembly of the destruction complex and recruitment of AXIN to the membrane / Intraflagellar transport / nitrogen cycle metabolic process / regulation of epithelial cell differentiation / centriole-centriole cohesion / protein localization to cell junction / Deactivation of the beta-catenin transactivating complex / intraciliary transport / anterograde dendritic transport of neurotransmitter receptor complex / Ovarian tumor domain proteases / microtubule anchoring at centrosome / Kinesins / negative regulation of cell cycle G1/S phase transition / Scrib-APC-beta-catenin complex / cilium movement / inner ear receptor cell stereocilium organization / negative regulation of cyclin-dependent protein serine/threonine kinase activity / photoreceptor connecting cilium / Degradation of beta-catenin by the destruction complex / proximal/distal pattern formation / COPI-dependent Golgi-to-ER retrograde traffic / negative regulation of epithelial cell proliferation involved in prostate gland development / motile cilium assembly / gamma-catenin binding / negative regulation of cardiac muscle cell proliferation / regulation of attachment of spindle microtubules to kinetochore / Hedgehog 'off' state / cell body fiber / cilium organization / positive regulation of pseudopodium assembly / positive regulation of intracellular protein transport / metaphase/anaphase transition of mitotic cell cycle / ribbon synapse / positive regulation of protein localization to centrosome / cell projection membrane / regulation of osteoclast differentiation / pattern specification process / negative regulation of microtubule depolymerization / dentate gyrus development / beta-catenin destruction complex / MHC class II antigen presentation / catenin complex / anterograde axonal transport / microtubule plus-end binding / protein kinase regulator activity / dorsal/ventral pattern formation / non-motile cilium assembly / motile cilium / regulation of microtubule-based process / determination of left/right symmetry / cell fate specification / anterior/posterior pattern specification / neural tube development / neural precursor cell proliferation / protein-containing complex localization / microtubule motor activity / kinesin complex / microtubule-based movement / skin development / dorsal/ventral neural tube patterning / smoothened signaling pathway / spectrin binding / negative regulation of G1/S transition of mitotic cell cycle / muscle cell cellular homeostasis / mitotic spindle assembly checkpoint signaling / regulation of osteoblast differentiation / stem cell population maintenance / positive regulation of cytokinesis / heart looping / forebrain development / neuron projection terminus / ciliary transition zone / establishment or maintenance of cell polarity / negative regulation of Wnt signaling pathway / mitotic cytokinesis / regulation of cell differentiation / positive regulation of cell division / dynein complex binding / somatic stem cell population maintenance / cilium assembly / epidermis development / lateral plasma membrane / hair follicle development / mitotic spindle assembly / bicellular tight junction
Similarity search - Function
Kinesin-associated protein 3 / Kinesin-associated protein (KAP) / Kinesin-associated protein (KAP) / Adenomatous polyposis coli protein repeat / SAMP / EB-1 binding / Adenomatous polyposis coli protein basic domain / Adenomatous polyposis coli protein, 15 residue repeat / Adenomatous polyposis coli (APC) family / Adenomatous polyposis coli protein ...Kinesin-associated protein 3 / Kinesin-associated protein (KAP) / Kinesin-associated protein (KAP) / Adenomatous polyposis coli protein repeat / SAMP / EB-1 binding / Adenomatous polyposis coli protein basic domain / Adenomatous polyposis coli protein, 15 residue repeat / Adenomatous polyposis coli (APC) family / Adenomatous polyposis coli protein / Adenomatous polyposis coli, N-terminal dimerisation domain / APC, N-terminal coiled-coil domain superfamily / Adenomatous polyposis coli (APC) repeat / APC repeat / SAMP Motif / EB-1 Binding Domain / APC basic domain / APC 15 residue motif / Adenomatous polyposis coli tumour suppressor protein / Armadillo-associated region on APC / Unstructured region on APC between 1st and 2nd catenin-bdg motifs / Unstructured region on APC between 1st two creatine-rich regions / Unstructured region on APC between APC_crr and SAMP / Unstructured region on APC between SAMP and APC_crr / Unstructured region on APC between APC_crr regions 5 and 6 / Coiled-coil N-terminus of APC, dimerisation domain / Adenomatous polyposis coli (APC) repeat / Kinesin-like protein / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Armadillo/beta-catenin-like repeats / Armadillo / Kinesin motor domain superfamily / Armadillo-like helical / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Kinesin-like protein KIF3A / Kinesin-associated protein 3 / Adenomatous polyposis coli protein / Kinesin-like protein KIF3B
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsJiang X / Danev R / Yanagisawa H / Kikkawa M
Funding support Japan, 4 items
OrganizationGrant numberCountry
Japan Science and TechnologyJPMJER2202 Japan
Japan Society for the Promotion of Science (JSPS)JP21H05247 Japan
Japan Society for the Promotion of Science (JSPS)JP24KF0141 Japan
Japan Society for the Promotion of Science (JSPS)JP24K18106 Japan
CitationJournal: Sci Adv / Year: 2025
Title: The hook-like adaptor and cargo-binding (HAC) domain in the kinesin-2 tail enables adaptor assembly and cargo recognition.
Authors: Xuguang Jiang / Radostin Danev / Sotaro Ichinose / Baichun Niu / Sumio Ohtsuki / Haruaki Yanagisawa / Satoru Nagatoishi / Kouhei Tsumoto / Nobutaka Hirokawa / Masahide Kikkawa /
Abstract: Intracellular transport relies on motor proteins such as kinesins to deliver cargo along microtubules, yet how they recognize cargo remains unclear. Here, we present high-resolution cryo-electron ...Intracellular transport relies on motor proteins such as kinesins to deliver cargo along microtubules, yet how they recognize cargo remains unclear. Here, we present high-resolution cryo-electron microscopy structures of the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3) bound to the cargo protein APC. Our findings reveal a previously uncharacterized KIF3 tail hook-like motif, termed the "HAC" domain, which mediates binding to both KAP3 adaptor and APC cargo. Within this domain, the KIF3A helical regions ensure cargo specificity, while a β-hairpin and KIF3B provide structural support. Biochemical and neuronal experiments confirm its functional importance. Notably, the HAC/KAP3 structure resembles hook-like architectures seen in kinesin-1 and dynein, suggesting a shared cargo recognition framework. These findings also shed light on kinesin-2 cargo specificity and offer a structural framework for understanding related neuronal transport mechanisms.
History
DepositionAug 10, 2025-
Header (metadata) releaseOct 1, 2025-
Map releaseOct 1, 2025-
UpdateNov 5, 2025-
Current statusNov 5, 2025Processing site: PDBj / Status: Released

-
Structure visualization

Supplemental images

emd_65778.png

Downloads & links

-
Map

FileDownload / File: emd_65778.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.3 Å/pix.
x 160 pix.
= 208. Å		1.3 Å/pix.
x 160 pix.
= 208. Å		1.3 Å/pix.
x 160 pix.
= 208. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.3 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.007
Minimum - Maximum-0.0017263165 - 2.4871056
Average (Standard dev.)0.0019050711 (±0.029757828)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions160160160
Spacing160160160
CellA=B=C: 208.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: raw map

Fileemd_65778_additional_1.map
Annotationraw map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: halfmap2

Fileemd_65778_half_map_1.map
Annotationhalfmap2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: halfmap1

Fileemd_65778_half_map_2.map
Annotationhalfmap1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC

EntireName: Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC
Components
  • Complex: Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC
    • Protein or peptide: Kinesin-like protein KIF3A
    • Protein or peptide: Kinesin-like protein KIF3B, N-terminally processed
    • Protein or peptide: Kinesin-associated protein 3
    • Protein or peptide: Adenomatous polyposis coli protein

-
Supramolecule #1: Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC

SupramoleculeName: Tetrameric complex of kinesin-2 KIF3A/B/KAP3 and cargo APC
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 220 KDa

-
Macromolecule #1: Kinesin-like protein KIF3A

MacromoleculeName: Kinesin-like protein KIF3A / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 21.084143 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSSHHHHHH SQSLQEEAQG KTKKLKKVWT MLMAAKSEMA DLQQEHQREI EGLLENIRQL SRELRLQMLI IDNFIPQDYQ EMIENYVHW NEDIGEWQLK CVAYTGNNMR KQTPVPDKKE RDPFEVDLSH VYLAYTEESL RQSLMKLERP RTSKGKARPK M GRRKRSAK PETVIDSLLQ

UniProtKB: Kinesin-like protein KIF3A

-
Macromolecule #2: Kinesin-like protein KIF3B, N-terminally processed

MacromoleculeName: Kinesin-like protein KIF3B, N-terminally processed / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 25.440057 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSLQQEVDIK TKKLKKLFSK LQAVKAEIHD LQEEHIKERQ ELEQTQNELT RELKLKHLII ENFIPLEEKN KIMNRSFFDD EEDHWKLHP ITRLENQQMM KRPVSAVGYK RPLSQHARMS MMIRPEPRYR AENIMLLELD MPSRTTRDYE GPAISPKVQA A LDAALQDE ...String:
MSLQQEVDIK TKKLKKLFSK LQAVKAEIHD LQEEHIKERQ ELEQTQNELT RELKLKHLII ENFIPLEEKN KIMNRSFFDD EEDHWKLHP ITRLENQQMM KRPVSAVGYK RPLSQHARMS MMIRPEPRYR AENIMLLELD MPSRTTRDYE GPAISPKVQA A LDAALQDE DEIQVDASSF ESTASRKPKA RPKSGRKSGS SSSSSGNPAS QFYPQSRGLV PK

UniProtKB: Kinesin-like protein KIF3B

-
Macromolecule #3: Kinesin-associated protein 3

MacromoleculeName: Kinesin-associated protein 3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 80.224148 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MQGEDARYLK RKVKGGNIDV HPSEKALIVQ YEVEATILGE MGDPMLGERK ECQKIIRLKS LNANTDITSL ARKVVEECKL IHPSKLSEV EQLLYYLQNR RDSLPGKEKK EKSSKPKDPP PFEGMEIDEV ANINDMDEYI ELLYEDIPDK VRGSALILQL A RNPDNLEE ...String:
MQGEDARYLK RKVKGGNIDV HPSEKALIVQ YEVEATILGE MGDPMLGERK ECQKIIRLKS LNANTDITSL ARKVVEECKL IHPSKLSEV EQLLYYLQNR RDSLPGKEKK EKSSKPKDPP PFEGMEIDEV ANINDMDEYI ELLYEDIPDK VRGSALILQL A RNPDNLEE LLLNETALGA LARVLREDWK QSVELATNII YIFFCFSSFS HFHGLITHYK IGALCMNIID HELKRHELWQ EE LSKKKKA VDEDLENQTL RKDYDKTFKK YQGLVVKQEQ LLRVALYLLL NLAEDTRTEL KMRNKNIVHM LVKALDRDNF ELL ILVVSF LKKLSIFMEN KNDMVEMDIV EKLVKMIPCE HEDLLNITLR LLLNLSFDTG LRNKMVQVGL LPKLTALLGN ENYK QIAMC VLYHISMDDR FKSMFAYTDC IPQLMKMLFE CSDERIDLEL ISFCINLAAN KRNVQLICEG NGLKMLMKRA LKLKD PLLM KMIRNISQHD GPTKNLFIDY VGDLAAQISS DEEEEFVIEC LGTLANLTIP DLDWELVLKE YKLVPFLKDK LKPGAA EDD LVLEVVIMIG TVSMDDSCAA LLAKSGIIPA LIELLNAQQE DDEFVCQIIY VFYQMVFHQA TRDVIIKETQ APAYLID LM HDKNNEIRKV CDNTLDIIAE YDEEWAKKIQ SEKFRWHNSQ WLEMVESRQL D

UniProtKB: Kinesin-associated protein 3

-
Macromolecule #4: Adenomatous polyposis coli protein

MacromoleculeName: Adenomatous polyposis coli protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 75.417633 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHSQD SCISMRQSGC LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCW EWQEAHEQGM DQDKNPMPAP VEHQICPAVC VLMKLSFDEE HRHAMNELGG LQAIAELLQV DCEMYGLTND H YSVTLRRY ...String:
MHHHHHHSQD SCISMRQSGC LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCW EWQEAHEQGM DQDKNPMPAP VEHQICPAVC VLMKLSFDEE HRHAMNELGG LQAIAELLQV DCEMYGLTND H YSVTLRRY AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL QQVIASVLRN LSWRADVNSK KTLREVGSVK AL MECALEV KKESTLKSVL SALWNLSAHC TENKADICAV DGALAFLVGT LTYRSQTNTL AIIESGGGIL RNVSSLIATN EDH RQILRE NNCLQTLLQH LKSHSLTIVS NACGTLWNLS ARNPKDQEAL WDMGAVSMLK NLIHSKHKMI AMGSAAALRN LMAN RPAKY KDANIMSPGS SLPSLHVRKQ KALEAELDAQ HLSETFDNID NLSPKASHRS KQRHKQNLYG DYAFDANRHD DSRSD NFNT GNMTVLSPYL NTTVLPSSSS SRGSLDSSRS EKDRSLERER GIGLSAYHPT TENAGTSSKR GLQITTTAAQ IAKVME EVS AIHTSQDDRS SASTTEFHCV ADDRSAARRS SASHTHSNTY NFTKSENSNR TCSMPYAKVE YKRSSNDSLN SVTSSDG YG KRGQMKPSVE SYSEDDESKF CSYGQYPADL AHKIHSAN

UniProtKB: Adenomatous polyposis coli protein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.0375 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 120 sec.
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 279 K / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy #1

Microscopy ID1
MicroscopeJEOL CRYO ARM 200
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingImage recording ID: 1 / Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 36020 / Average electron dose: 64.7 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 1.55 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 80000
Sample stageCooling holder cryogen: NITROGEN

-
Electron microscopy #1~

Microscopy ID1
MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingImage recording ID: 2 / Film or detector model: GATAN K3 (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Number grids imaged: 1 / Number real images: 19918 / Average electron dose: 63.0 e/Å2
Details: tilted-stage image collection with tilt angles of 30 and 40 degrees
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Image recording ID1
Particle selectionNumber selected: 12833027
CTF correctionSoftware - Name: cryoSPARC / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: Ab-Initio Reconstruction
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 407310
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC
Final 3D classificationNumber classes: 4 / Software - Name: cryoSPARC
FSC plot (resolution estimation)

-
Atomic model buiding 1

Initial model
PDB IDChainDetails

9w9h

source_name: PDB, initial_model_type: experimental modelchains, A-C

4yje

source_name: PDB, initial_model_type: experimental modelchain D
DetailsInitial local fitting was done using Phenix dock-in-map tool.
RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-9w9i:
Cryo-EM structure of the kinesin-2 tail domain in complex with KAP3 and APC

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more