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- PDB-7og1: AP2 clathrin adaptor core in complex with cargo peptide and FCHO2 -

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Basic information

Entry
Database: PDB / ID: 7og1
TitleAP2 clathrin adaptor core in complex with cargo peptide and FCHO2
Components
  • (AP-2 complex subunit ...) x 4
  • F-BAR domain only protein 2
  • TGN38 CARGO PEPTIDE
KeywordsENDOCYTOSIS / clathrin-mediated endocytosis (CME) / protein recycling / plasma membrane
Function / homology
Function and homology information


membrane invagination / Gap junction degradation / Formation of annular gap junctions / presynaptic endocytic zone membrane / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / WNT5A-dependent internalization of FZD4 / Retrograde neurotrophin signalling ...membrane invagination / Gap junction degradation / Formation of annular gap junctions / presynaptic endocytic zone membrane / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / WNT5A-dependent internalization of FZD4 / Retrograde neurotrophin signalling / VLDLR internalisation and degradation / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors / Retrograde neurotrophin signalling / clathrin adaptor complex / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Trafficking of GluR2-containing AMPA receptors / extrinsic component of presynaptic endocytic zone membrane / VLDLR internalisation and degradation / WNT5A-dependent internalization of FZD4 / MHC class II antigen presentation / Recycling pathway of L1 / AP-2 adaptor complex / regulation of vesicle size / postsynaptic neurotransmitter receptor internalization / Recycling pathway of L1 / LDL clearance / clathrin coat assembly / Cargo recognition for clathrin-mediated endocytosis / Retrograde neurotrophin signalling / Cargo recognition for clathrin-mediated endocytosis / clathrin-coated endocytic vesicle / Clathrin-mediated endocytosis / clathrin adaptor activity / Clathrin-mediated endocytosis / positive regulation of synaptic vesicle endocytosis / membrane coat / vesicle budding from membrane / clathrin-dependent endocytosis / coronary vasculature development / MHC class II antigen presentation / endolysosome membrane / signal sequence binding / Nef Mediated CD4 Down-regulation / aorta development / clathrin-coated vesicle / ventricular septum development / low-density lipoprotein particle receptor binding / Neutrophil degranulation / clathrin binding / phosphatidylserine binding / positive regulation of receptor internalization / Trafficking of GluR2-containing AMPA receptors / Recycling pathway of L1 / synaptic vesicle endocytosis / EPH-ephrin mediated repulsion of cells / negative regulation of protein localization to plasma membrane / protein serine/threonine kinase binding / clathrin-coated pit / phosphatidylinositol-4,5-bisphosphate binding / vesicle-mediated transport / MHC class II antigen presentation / VLDLR internalisation and degradation / phosphatidylinositol binding / kidney development / protein localization to plasma membrane / intracellular protein transport / clathrin-coated endocytic vesicle membrane / kinase binding / terminal bouton / receptor internalization / cytoplasmic side of plasma membrane / disordered domain specific binding / endocytic vesicle membrane / Cargo recognition for clathrin-mediated endocytosis / synaptic vesicle / Clathrin-mediated endocytosis / presynapse / cytoplasmic vesicle / protein-containing complex assembly / postsynapse / transmembrane transporter binding / Potential therapeutics for SARS / protein domain specific binding / intracellular membrane-bounded organelle / lipid binding / glutamatergic synapse / synapse / protein-containing complex binding / protein kinase binding / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
F-BAR domain only protein 2 / GEM-interacting protein-like, FCH domain / Muniscin C-terminal / Muniscin C-terminal mu homology domain / AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal ...F-BAR domain only protein 2 / GEM-interacting protein-like, FCH domain / Muniscin C-terminal / Muniscin C-terminal mu homology domain / AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal / Fes/CIP4 homology domain / FCH domain / F-BAR domain / F-BAR domain profile. / Adaptor protein complex, sigma subunit / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta-adaptin appendage, C-terminal subdomain / AP-1/2/4 complex subunit beta / Beta2-adaptin appendage, C-terminal sub-domain / Beta2-adaptin appendage, C-terminal sub-domain / AP complex subunit beta / : / Clathrin adaptor complex, small chain / Clathrin adaptor complexes small chain signature. / Clathrin adaptor complexes medium chain signature 1. / Clathrin adaptor, mu subunit / Clathrin adaptor, mu subunit, conserved site / Clathrin adaptor complexes medium chain signature 2. / : / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Adaptor complexes medium subunit family / AP complex, mu/sigma subunit / Clathrin adaptor complex small chain / AP-2 complex subunit mu, C-terminal superfamily / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Mu homology domain / Adaptin C-terminal domain / Mu homology domain (MHD) profile. / Adaptin C-terminal domain / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Longin-like domain superfamily / AH/BAR domain superfamily / TBP domain superfamily / Armadillo/beta-catenin-like repeats / Armadillo / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
AP-2 complex subunit alpha-2 / AP-2 complex subunit sigma / AP-2 complex subunit beta / AP-2 complex subunit mu / F-BAR domain only protein 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Homo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsZaccai, N.R. / Kelly, B.T. / Evans, P.R. / Owen, D.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome Trust207455/Z/17/Z United Kingdom
Citation
Journal: Sci Adv / Year: 2022
Title: FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P-dependent switch.
Authors: Nathan R Zaccai / Zuzana Kadlecova / Veronica Kane Dickson / Kseniya Korobchevskaya / Jan Kamenicky / Oleksiy Kovtun / Perunthottathu K Umasankar / Antoni G Wrobel / Jonathan G G Kaufman / ...Authors: Nathan R Zaccai / Zuzana Kadlecova / Veronica Kane Dickson / Kseniya Korobchevskaya / Jan Kamenicky / Oleksiy Kovtun / Perunthottathu K Umasankar / Antoni G Wrobel / Jonathan G G Kaufman / Sally R Gray / Kun Qu / Philip R Evans / Marco Fritzsche / Filip Sroubek / Stefan Höning / John A G Briggs / Bernard T Kelly / David J Owen / Linton M Traub /
Abstract: Clathrin-mediated endocytosis (CME) is the main mechanism by which mammalian cells control their cell surface proteome. Proper operation of the pivotal CME cargo adaptor AP2 requires membrane- ...Clathrin-mediated endocytosis (CME) is the main mechanism by which mammalian cells control their cell surface proteome. Proper operation of the pivotal CME cargo adaptor AP2 requires membrane-localized Fer/Cip4 homology domain-only proteins (FCHO). Here, live-cell enhanced total internal reflection fluorescence-structured illumination microscopy shows that FCHO marks sites of clathrin-coated pit (CCP) initiation, which mature into uniform-sized CCPs comprising a central patch of AP2 and clathrin corralled by an FCHO/Epidermal growth factor potential receptor substrate number 15 (Eps15) ring. We dissect the network of interactions between the FCHO interdomain linker and AP2, which concentrates, orients, tethers, and partially destabilizes closed AP2 at the plasma membrane. AP2's subsequent membrane deposition drives its opening, which triggers FCHO displacement through steric competition with phosphatidylinositol 4,5-bisphosphate, clathrin, cargo, and CME accessory factors. FCHO can now relocate toward a CCP's outer edge to engage and activate further AP2s to drive CCP growth/maturation.
#1: Journal: Acta Crystallogr., Sect. D: Biol. Crystallogr. / Year: 2012
Title: Towards automated crystallographic structure refinement with phenix.refine.
Authors: Afonine, P.V.
History
DepositionMay 5, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 1, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Derived calculations / Refinement description
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AAA: AP-2 complex subunit alpha-2
BBB: AP-2 complex subunit beta
MMM: AP-2 complex subunit mu
SSS: AP-2 complex subunit sigma
GGG: F-BAR domain only protein 2
CCC: AP-2 complex subunit mu
PPP: TGN38 CARGO PEPTIDE
DDD: F-BAR domain only protein 2


Theoretical massNumber of molelcules
Total (without water)290,7688
Polymers290,7688
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: immunoprecipitation, surface plasmon resonance
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23840 Å2
ΔGint-101 kcal/mol
Surface area76600 Å2
Unit cell
Length a, b, c (Å)92.576, 150.070, 96.430
Angle α, β, γ (deg.)90.000, 112.652, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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AP-2 complex subunit ... , 4 types, 5 molecules AAABBBMMMCCCSSS

#1: Protein AP-2 complex subunit alpha-2 / 100 kDa coated vesicle protein C / Adaptor protein complex AP-2 subunit alpha-2 / Adaptor-related ...100 kDa coated vesicle protein C / Adaptor protein complex AP-2 subunit alpha-2 / Adaptor-related protein complex 2 subunit alpha-2 / Alpha-adaptin C / Alpha2-adaptin / Clathrin assembly protein complex 2 alpha-C large chain / Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit


Mass: 69656.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ap2a2, Adtab / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: P18484
#2: Protein AP-2 complex subunit beta / AP105B / Adaptor protein complex AP-2 subunit beta / Adaptor-related protein complex 2 subunit beta ...AP105B / Adaptor protein complex AP-2 subunit beta / Adaptor-related protein complex 2 subunit beta / Beta-2-adaptin / Beta-adaptin / Clathrin assembly protein complex 2 beta large chain / Plasma membrane adaptor HA2/AP2 adaptin beta subunit


Mass: 66953.195 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AP2B1, ADTB2, CLAPB1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: P63010
#3: Protein AP-2 complex subunit mu / AP-2 mu chain / Adaptor protein complex AP-2 subunit mu / Adaptor-related protein complex 2 subunit ...AP-2 mu chain / Adaptor protein complex AP-2 subunit mu / Adaptor-related protein complex 2 subunit mu / Clathrin assembly protein complex 2 mu medium chain / Clathrin coat assembly protein AP50 / Clathrin coat-associated protein AP50 / Mu2-adaptin / Plasma membrane adaptor AP-2 50 kDa protein


Mass: 51044.113 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ap2m1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: P84092
#4: Protein AP-2 complex subunit sigma / Adaptor protein complex AP-2 subunit sigma / Adaptor-related protein complex 2 subunit sigma / ...Adaptor protein complex AP-2 subunit sigma / Adaptor-related protein complex 2 subunit sigma / Clathrin assembly protein 2 sigma small chain / Clathrin coat assembly protein AP17 / Clathrin coat-associated protein AP17 / Plasma membrane adaptor AP-2 17 kDa protein / Sigma-adaptin 3b / Sigma2-adaptin


Mass: 17038.688 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ap2s1, Ap17, Claps2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: P62743

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Protein / Protein/peptide , 2 types, 3 molecules GGGDDDPPP

#5: Protein F-BAR domain only protein 2


Mass: 17111.500 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FCHO2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: Q0JRZ9
#6: Protein/peptide TGN38 CARGO PEPTIDE


Mass: 808.860 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)

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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: 2.56 Å3/Da / Density % sol: 51.99 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop
Details: Crystals of AP-2 in complex with FCHO2 linker and TGN38 peptide, supplemented with 10mM K Na Tartrate, grew in sitting drops with reservoir 0.1M Mg formate dehydrate, 10% to 15% PEG 3350. ...Details: Crystals of AP-2 in complex with FCHO2 linker and TGN38 peptide, supplemented with 10mM K Na Tartrate, grew in sitting drops with reservoir 0.1M Mg formate dehydrate, 10% to 15% PEG 3350. The crystals were cryo-protected with 0.1M Mg formate dehydrate, 13% PEG 3350, 18-24% Glycerol and 1mg/ml of peptide.
Temp details: Room temperature

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.92001 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Apr 28, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.92001 Å / Relative weight: 1
ReflectionResolution: 3.25→78.58 Å / Num. obs: 38355 / % possible obs: 100 % / Redundancy: 6.6 % / CC1/2: 0.998 / Rmerge(I) obs: 0.133 / Rpim(I) all: 0.086 / Rrim(I) all: 0.159 / Net I/σ(I): 7.2
Reflection shellResolution: 3.25→3.39 Å / Redundancy: 6 % / Rmerge(I) obs: 2.123 / Mean I/σ(I) obs: 0.8 / Num. unique obs: 4690 / CC1/2: 0.366 / Rpim(I) all: 1.465 / Rrim(I) all: 2.59 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
PHASERphasing
PHENIXv1.19refinement
Aimlessdata scaling
DIALSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2xa7

2xa7


Resolution: 3.25→76.662 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.903 / SU B: 44.28 / SU ML: 0.687 / Cross valid method: FREE R-VALUE / ESU R Free: 0.636
RfactorNum. reflection% reflection
Rfree0.3063 1881 4.908 %
Rwork0.2066 36445 -
all0.212 --
obs-38326 99.924 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 135.397 Å2
Baniso -1Baniso -2Baniso -3
1--2.812 Å20 Å23.095 Å2
2---4.448 Å20 Å2
3---3.469 Å2
Refinement stepCycle: LAST / Resolution: 3.25→76.662 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14392 0 0 0 14392
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01314644
X-RAY DIFFRACTIONr_bond_other_d0.0020.01714362
X-RAY DIFFRACTIONr_angle_refined_deg1.5781.63819814
X-RAY DIFFRACTIONr_angle_other_deg1.1151.57933058
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.29151794
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.55922.766752
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.635152712
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.691591
X-RAY DIFFRACTIONr_chiral_restr0.0610.21947
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0216315
X-RAY DIFFRACTIONr_gen_planes_other0.0020.023251
X-RAY DIFFRACTIONr_nbd_refined0.2410.24102
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1990.215817
X-RAY DIFFRACTIONr_nbtor_refined0.1710.26690
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0790.27862
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1960.2499
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0710.215
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2610.211
X-RAY DIFFRACTIONr_nbd_other0.2060.276
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.0040.21
X-RAY DIFFRACTIONr_mcbond_it12.12814.3417206
X-RAY DIFFRACTIONr_mcbond_other12.12614.347205
X-RAY DIFFRACTIONr_mcangle_it18.68621.4718990
X-RAY DIFFRACTIONr_mcangle_other18.68521.4728991
X-RAY DIFFRACTIONr_scbond_it10.8214.6987438
X-RAY DIFFRACTIONr_scbond_other10.81914.6987438
X-RAY DIFFRACTIONr_scangle_it17.11721.85210824
X-RAY DIFFRACTIONr_scangle_other17.11621.85210825
X-RAY DIFFRACTIONr_lrange_it23.935167.54616853
X-RAY DIFFRACTIONr_lrange_other23.935167.54516853
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.25-3.3340.4381520.3732669X-RAY DIFFRACTION99.6116
3.334-3.4250.3831370.3632621X-RAY DIFFRACTION100
3.425-3.5250.3561320.312529X-RAY DIFFRACTION100
3.525-3.6330.4181140.2792461X-RAY DIFFRACTION100
3.633-3.7520.3641130.2422444X-RAY DIFFRACTION100
3.752-3.8830.3591180.2432320X-RAY DIFFRACTION100
3.883-4.0290.3251130.2262243X-RAY DIFFRACTION100
4.029-4.1940.3061010.1892166X-RAY DIFFRACTION100
4.194-4.380.2971070.1862059X-RAY DIFFRACTION99.9539
4.38-4.5930.3421010.1761976X-RAY DIFFRACTION100
4.593-4.8410.291850.171882X-RAY DIFFRACTION99.9492
4.841-5.1330.233820.1531784X-RAY DIFFRACTION100
5.133-5.4860.3441110.1951651X-RAY DIFFRACTION100
5.486-5.9240.446660.2481576X-RAY DIFFRACTION100
5.924-6.4870.356720.1971444X-RAY DIFFRACTION100
6.487-7.2480.295730.1911294X-RAY DIFFRACTION100
7.248-8.360.262730.1671156X-RAY DIFFRACTION100
8.36-10.2160.222620.142965X-RAY DIFFRACTION100
10.216-14.3530.193420.147768X-RAY DIFFRACTION100
14.353-76.660.36270.348437X-RAY DIFFRACTION99.5708

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